Solution structure and backbone dynamics of the K18G/R82E Alicyclobacillus acidocaldarius thioredoxin mutant: A molecular analysis of its reduced thermal stability
Solution structure and backbone dynamics of the K18G/R82E Alicyclobacillus acidocaldarius thioredoxin mutant: A molecular analysis of its reduced thermal stability(438 views) Leone M, Di Lello P, Ohlenschläger O, Pedone E, Bartolucci S, Rossi M, Di Blasio B, Pedone C, Saviano M, Isernia C, Fattorusso R
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2004 May 25; 43(20): 6043-6058.
Ist. di Biostrutture e Bioimmagini, Via Mezzocannone 6/8, 80134 Napoli, Italy
Dipartimento di Scienze Ambientali, Seconda Università di Napoli, via Vivaldi 43, 81100 Caserta, Italy
Institut fur Molec. Biotechnologie, Beutenbergstrasse 11, D-07745 Jena, Germany
Dipartimento di Chimica Biologica, Universita di Napoli Federico II, Via Mezzocannone 16, 80134 Napoli, Italy
References: Jaenicke, R., Protein stability and molecular adaptation to extreme conditions (1991) Eur. J. Biochem., 202, pp. 715-72
Jaenicke, R., Böhm, G., The stability of proteins in extreme environments (1998) Curr. Opin. Struct. Biol., 8, pp. 738-748
Creighton, T.E., (1993) Proteins: Structure and Molecular Properties, , W. H. Freeman, New York
Fersht, A., (1999) Structure and Mechanism in Protein Science, , W. H. Freeman, New York
Yano, J.K., Poulos, T.L., New understandings of thermostable and peizostable enzymes (2003) Curr. Opin. Biotechnol., 14, pp. 360-365
Zavodsky, P., Kardos, J., Svingor, A., Petsko, G.A., Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins (1998) Proc. Natl. Acad. Sci. U.S.A., 95, pp. 7406-7411
Perl, D., Schmid, F.X., Electrostatic stabilization of a thermophilic cold shock protein (2001) J. Mol. Biol., 313, pp. 343-357
Holmgren, A., Thioredoxin (1985) Annu. Rev. Biochem., 54, pp. 237-271
Katti, S.K., LeMaster, D.M., Eklund, H., Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution (1990) J. Mol. Biol., 212, pp. 167-184
Holmgren, A., Söderberg, B.O., Eklund, H., Branden, C.I., Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 Å resolution (1975) Proc. Natl. Acad. Sci. U.S.A., 72, pp. 2305-2309
Qin, J., Clore, G.M., Gronenborn, A.M., The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin (1994) Structure, 2, pp. 503-522
Jeng, M.F., Campbell, A.P., Begley, T., Holmgren, A., Case, D.A., Wright, P.E., Dyson, H.J., High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin (1994) Structure, 2, pp. 853-868
Mittard, V., Blackledge, M.J., Stein, M., Jacquot, J.P., Marion, D., Lancelin, J.M., NMR solution structure of an oxidised thioredoxin h from the eukaryotic green alga Chlamydomonas reinhardtii (1997) Eur. J. Biochem., 243, pp. 374-383
Nicastro, G., De Chiara, C., Pedone, E., Tato, M., Rossi, M., Bartolucci, S., NMR solution structure of a novel thioredoxin from Bacillus acidocaldarius possible determinants of protein stability (2000) Eur. J. Biochem., 267, pp. 403-413
Lancelin, J.M., Guilhaudis, L., Krimm, I., Blackledge, M.J., Marion, D., Jacquot, J.P., NMR structures of thioredoxin m from the green alga Chlamydomonas reinhardtii (2000) Proteins, 41, pp. 334-349
Neira, J.M., Gonzales, C., Toiron, C., De Prat-Gay, G., Rico, M., Three-dimensional solution structure and stability of thioredoxin m from spinach (2001) Biochemistry, 40, pp. 146-156
Dangi, B., Dobrodumov, A.V., Louis, J.M., Gronenborn, A.M., Solution structure and dynamics of the human-Escherichia coli thioredoxin chimera: Insights into thermodynamic stability (2002) Biochemistry, 41, pp. 9376-9388
Stone, M.J., Chandrasekhar, K., Holmgren, A., Wright, P.E., Dyson, H.J., Comparison of backbone and tryptophan side-chain dynamics of reduced and oxidized Escherichia coli thioredoxin using 15N NMR relaxation measurements (1993) Biochemistry, 32, pp. 426-435
Eklund, H., Gleason, F.K., Holmgren, A., Structural and functional relations among thioredoxins of different species (1991) Proteins, 11, pp. 13-28
Bartolucci, S., Guagliardi, A., Pedone, E., De Pasquale, D., Cannio, R., Camardella, L., Rossi, M., Nicolini, C., Thioredoxin from Bacillus acidocaldarius: Characterization, high-level expression in Escherichia coli and molecular modelling (1997) Biochem. J., 328, pp. 277-285
Pedone, E., Bartolucci, S., Rossi, M., Saviano, M., Computational analysis of the thermal stability in thioredoxins: A molecular dynamics approach (1998) J. Biomol. Struct. Dyn., 16, pp. 437-446
Pedone, E., Cannio, R., Saviano, M., Rossi, M., Bartolucci, S., Prediction and experimental testing of Bacillus acidocaldarius thioredoxin stability (1999) Biochem. J., 339, pp. 309-317
Pedone, E., Saviano, M., Rossi, M., Bartolucci, S., A single point mutation (Glu85Arg) increases the stability of the thioredoxin from Escherichia coli (2001) Protein Eng., 14, pp. 255-260
Zhang, O., Kay, L.E., Olivier, J.P., Forman-Kay, J.D., Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques (1994) J. Biomol. NMR, 4, pp. 845-858
Talluri, S., Wagner, G., An optimized 3D NOESY-HSQC (1996) J. Magn. Reson., 112, pp. 200-205
Vuister, G.W., Bax, A., A quantitative J correlation: A new approach for measuring homonuclear three-bond J(HNHα) coupling constants in 15N-enriched proteins (1993) J. Am. Chem. Soc., 115, pp. 7772-7777
Archer, S.J., Ikura, M., Torchia, D.A., Bax, A., An alternative 3D-NMR technique for correlating backbone N-15 with side chain H-beta-resonances in larger proteins (1991) J. Magn. Reson., 95, pp. 636-641
Wilker, W., Leibfritz, D., Kerssebaum, R., Bermel, W., Gradient selection in inverse heteronuclear correlation spectroscopy (1993) Magn. Reson. Chem., 31, pp. 287-292
Griesinger, C., Otting, G., Wüthrich, K., Ernst, R.R., Clean TOCSY for 1H spin system identification in macromolecules (1988) J. Am. Chem. Soc., 110, p. 7870
Kumar, A., Ernst, R.R., Wüthrich, K., A two-dimensional nuclear overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules (1980) Biochem. Biophys. Res. Commun., 95, pp. 1-6
Rance, M., Sörensen, O.W., Bodenhausen, G., Wagner, G., Ernst, R.R., Wüthrich, K., Improved spectral resolution in COSY 1H NMR spectra of proteins via double quantum filtering (1983) Biochem. Biophys. Res. Commun., 117, pp. 479-485
Cavanagh, J., Rance, M., Suppression of cross-relaxation effects in TOCSY spectra via a modified dipsi-2 mixing sequence (1992) J. Magn. Reson., 96, pp. 670-678
Kay, L.E., Keifer, P., Saarinen, T., Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity (1992) J. Am. Chem. Soc., 114, pp. 10663-10665
Bartels, C., Xia, T., Billeter, M., Wüthrich, K., The program XEASY for computer-supported NMR spectral analysis of biological macromolecules (1995) J. Biomol. NMR, 5, pp. 1-10
Farrow, N.A., Muhandiram, R., Singer, A.U., Pascal, S.M., Kay, C.M., Gish, G., Shoelson, S.E., Kay, L.E., Backbone dynamics of a free and phosphorpeptidecomplexed Src homology 2 domain studied by 15N NMR relaxation (1994) Biochemistry, 33, pp. 5984-6003
Shapiro, Y.E., Sinev, M.A., Sineva, E.V., Tugarinov, V., Meirovitch, E., Backbone dynamics of Escherichia coli adenylate kinase at the extreme stages of the catalytic cycle studied by 15N NMR relaxation (2000) Biochemistry, 39, pp. 6634-6644
Beeser, S.A., Goldenberg, D.P., Oas, T.G., Enhanced protein flexibility caused by a destabilizing amino acid replacement in BPTI (1997) J. Mol. Biol., 269, pp. 154-164
Viles, J.H., Duggan, B.M., Zaborowski, E., Schwarzinger, S., Huntley, J.J.A., Kroon, G.J.A., Dyson, H.J., Potential bias in NMR relaxation data introduced by peak intensity analysis and curve fitting methods (2001) J. Biomol. NMR, 21, pp. 1-9
Lee, L.K., Rance, M., Chazin, W.J., Palmer, A.G., Rotational diffusion anisotropy of proteins from simultaneous analysis of 15N and 13Cα nuclear spin relaxation (1997) J. Biomol. NMR, 9, pp. 287-298
Brüschweiler, R., Liao, X., Wright, P.E., Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling (1995) Science, 268, pp. 886-889
Tjandra, N., Feller, S.E., Pastor, R.W., Bax, A., Rotational diffusion anisotropy of human ubiquitin from 15N NMR relaxation (1995) J. Am. Chem Soc., 117, pp. 12562-12566
Lipari, G., Szabo, A., Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. Theory and range of validity (1982) J. Am. Chem. Soc., 104, pp. 4546-4559
Clore, G.M., Driscoll, P.C., Wingfield, P.T., Gronenborn, A.M., Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse detected heteronuclear 15N-1N NMR spectroscopy (1990) Biochemistry, 29, pp. 7387-7401
Barbato, G., Ikura, M., Kay, L.E., Pastor, R.W., Bax, A., Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible (1992) Biochemistry, 31, pp. 5269-5278
Mandel, A.M., Akke, M., Palmer, A.G., Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme (1995) J. Mol. Biol., 246, pp. 144-163
Clore, G.M., Szabo, A., Bax, A., Kay, L.E., Driscoll, P.C., Gronenborn, A.M., Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins (1990) J. Am. Chem. Soc., 112, pp. 4989-4991
Palmer, A.G., Rance, M., Wright, P.E., Intramolecular motions of a zinc finger DNA-binding domain from xfin characterized by proton-detected natural abundance 13C heteronuclear NMR spectroscopy (1991) J. Am. Chem. Soc., 113, pp. 4371-4380
Herrmann, T., Güntert, P., Wüthrich, K., Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA (2002) J. Mol. Biol., 319, pp. 209-227
Luginbühl, P., Güntert, P., Billeter, M., Wüthrich, K., The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules (1996) J. Biomol. NMR, 8, pp. 136-146
Koradi, R., Billeter, M., Wüthrich, K., MOLMOL: A program for display and analysis of macromolecular structures (1996) J. Mol. Graphics, 14, pp. 29-32
Laskowski, R.A., Rullmann, J.A., MacArthur, M.W., Kaptein, R., Thornton, J.M., AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR (1996) J. Biomol. NMR, 8, pp. 477-486
Güntert, P., Mumenthaler, C., Wüthrich, K., Torsion angle dynamics for NMR structure calculation with the new program DYANA (1997) J. Mol. Biol., 273, pp. 283-298
Bartolucci, S., De Simone, G., Galdiero, S., Improta, R., Menchise, V., Pedone, C., Pedone, E., Saviano, M., An integrated structural and computational study of the thermostability of two thioredoxin mutants from Alicyclobacillus acidocaldarius (2003) J. Bacteriol., 185, pp. 4285-4289
Martin, J.L., Thioredoxin a fold for all reasons (1995) Structure, 15, pp. 245-250
Kay, L.E., Torchia, D.A., Bax, A., Backbone dynamics of proteins as studied by nitrogen-15 inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease (1989) Biochemistry, 28, pp. 8972-8979
Chakravarty, S., Varadarajan, R., Elucidation of factors responsible for enhanced thermal stability of proteins: A structural genomics based study (2002) Biochemistry, 41, pp. 8152-8161
Szilagyi, A., Zavodszky, P., Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: Results of a comprehensive survey (2000) Struct. Folding Des., 8, pp. 493-504
Darland, G., Brock, T.D., Bacillus acidocaldarius sp. nov, an acidophilic thermophilic spore-forming bacterium (1971) J. Gen. Microbiol., 67, pp. 9-15
Landry, S.J., Steede, N.K., Maskos, K., Temperature dependence of backbone dynamics in loops of human mitochondrial heat shock protein 10 (1997) Biochemistry, 36, pp. 10975-10986
Bracken, C., Carr, P.A., Cavanagh, J., Palmer, A.G., Temperature dependence of intramolecular dynamics of the basic region leucine zipper of GCN4: Implications for the entropy of association with DNA (1999) J. Mol. Biol., 285, pp. 2133-2146
Evenäs, J., Forsén, S., Malmendal, A., Akke, M., Backbone dynamics and energetics of a calmodulin domain mutant exchanging between closed and open conformations (1999) J. Mol. Biol., 289, pp. 603-617
Bertini, I., Luchinat, C., Niikura, Y., Presenti, C., Model-free analysis of a thermophilic Fe7S8 protein compared with a mesophilic Fe4S4 protein (2000) Proteins, 41, pp. 75-85
Seewald, M.J., Pichumani, K., Stowell, C., Tibbals, B.V., Regan, L., Stone, M.J., The role of backbone conformational heat capacity in protein stability: Temperature-dependent dynamics of the B1 domain of Streptococcal protein G (2000) Protein Sci., 9, pp. 1177-1193
Lee, A.L., Sharp, K.A., Kranza, J.K., Song, X., Wand, A.J., Temperature dependence of the internal dynamics of a calmodulin-peptide complex (2002) Biochemistry, 41, pp. 13814-13825
Vugmeyster, L., Trott, O., McKnight, C.J., Raleigh, D.P., Palmer III, A.G., Temperature-dependent dynamics of the villin headpiece helical subdomain, an unusually small thermostable protein (2002) J. Mol. Biol., 320, pp. 841-854
Idiyatullin, D., Nesmelova, I., Daragan, V.A., Mayo, K., Heat capacities and a snapshot of the energy landscape in protein GB1 from the Pre-denaturation temperature dependence of backbone NH nanosecond fluctuations (2003) J. Mol. Biol., 325, pp. 149-162
Kovrigin, E.L., Cole, R., Loria, J.P., Temperature dependence of the backbone dynamics of Ribonuclease A in the ground state and bound to the inhibitor 5′-phosphorhymidine (3′-5′)pyrophosphatase adenosine 3′-phosphate (2003) Biochemistry, 42, pp. 5279-5291
Bhattacharya, S., Falzone, C., Lecomte, J., Backbone dynamics of apocytochrome b5 in its native, partially folded state (1999) Biochemistry, 38, pp. 2577-2589
Jin, C., Liao, X., Backbone dynamics of a winged helix protein and its DNA complex at different temperatures: Changes of internal motions in genesis upon binding to DNA (1999) J. Mol. Biol., 292, pp. 641-651
Meekhof, A.E., Freund, S.M., Probing residual structure and backbone dynamics on the milli- to picosecond time scale in a urea-denatured fibronectin type III domain (1999) J. Mol. Biol., 86, pp. 579-592
Stone, M.J., NMR relaxation studies of the role of conformational entropy in stability and ligand binding (2001) Acc. Chem. Res., 34, pp. 379-388
Wintrode, P.L., Zhang, D., Vaidehi, N., Arnold, F.H., Goddard III, W.A., Protein dynamics in a family of laboratory evolved thermophilic enzymes (2003) J. Mol. Biol., 327, pp. 745-757
Georgescu, R.E., Garcia-Mira, M.M., Tasayco, M.L., Sanchez-Ruiz, J.M., Heat capacity analysis of oxidized Escherichia coli thioredoxin fragments (1-73, 74-108) and their noncovalent complex. Evidence for the burial of apolar surface in protein unfolded states (2001) Eur. J. Biochem., 268, pp. 1477-1485
Jaenicke, R., B hm, G., The stability of proteins in extreme environments (1998) Curr. Opin. Struct. Biol., 8, pp. 738-748
Creighton, T. E., (1993) Proteins: Structure and Molecular Properties, , W. H. Freeman, New York
Yano, J. K., Poulos, T. L., New understandings of thermostable and peizostable enzymes (2003) Curr. Opin. Biotechnol., 14, pp. 360-365
Katti, S. K., LeMaster, D. M., Eklund, H., Crystal structure of thioredoxin from Escherichia coli at 1. 68 A resolution (1990) J. Mol. Biol., 212, pp. 167-184
Holmgren, A., S derberg, B. O., Eklund, H., Branden, C. I., Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2. 8 resolution (1975) Proc. Natl. Acad. Sci. U. S. A., 72, pp. 2305-2309
Qin, J., Clore, G. M., Gronenborn, A. M., The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin (1994) Structure, 2, pp. 503-522
Jeng, M. F., Campbell, A. P., Begley, T., Holmgren, A., Case, D. A., Wright, P. E., Dyson, H. J., High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin (1994) Structure, 2, pp. 853-868
Lancelin, J. M., Guilhaudis, L., Krimm, I., Blackledge, M. J., Marion, D., Jacquot, J. P., NMR structures of thioredoxin m from the green alga Chlamydomonas reinhardtii (2000) Proteins, 41, pp. 334-349
Neira, J. M., Gonzales, C., Toiron, C., De Prat-Gay, G., Rico, M., Three-dimensional solution structure and stability of thioredoxin m from spinach (2001) Biochemistry, 40, pp. 146-156
Stone, M. J., Chandrasekhar, K., Holmgren, A., Wright, P. E., Dyson, H. J., Comparison of backbone and tryptophan side-chain dynamics of reduced and oxidized Escherichia coli thioredoxin using 15N NMR relaxation measurements (1993) Biochemistry, 32, pp. 426-435
Zhang, O., Kay, L. E., Olivier, J. P., Forman-Kay, J. D., Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques (1994) J. Biomol. NMR, 4, pp. 845-858
Vuister, G. W., Bax, A., A quantitative J correlation: A new approach for measuring homonuclear three-bond J (HNH) coupling constants in 15N-enriched proteins (1993) J. Am. Chem. Soc., 115, pp. 7772-7777
Archer, S. J., Ikura, M., Torchia, D. A., Bax, A., An alternative 3D-NMR technique for correlating backbone N-15 with side chain H-beta-resonances in larger proteins (1991) J. Magn. Reson., 95, pp. 636-641
Rance, M., S rensen, O. W., Bodenhausen, G., Wagner, G., Ernst, R. R., W thrich, K., Improved spectral resolution in COSY 1H NMR spectra of proteins via double quantum filtering (1983) Biochem. Biophys. Res. Commun., 117, pp. 479-485
Kay, L. E., Keifer, P., Saarinen, T., Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity (1992) J. Am. Chem. Soc., 114, pp. 10663-10665
Farrow, N. A., Muhandiram, R., Singer, A. U., Pascal, S. M., Kay, C. M., Gish, G., Shoelson, S. E., Kay, L. E., Backbone dynamics of a free and phosphorpeptidecomplexed Src homology 2 domain studied by 15N NMR relaxation (1994) Biochemistry, 33, pp. 5984-6003
Shapiro, Y. E., Sinev, M. A., Sineva, E. V., Tugarinov, V., Meirovitch, E., Backbone dynamics of Escherichia coli adenylate kinase at the extreme stages of the catalytic cycle studied by 15N NMR relaxation (2000) Biochemistry, 39, pp. 6634-6644
Beeser, S. A., Goldenberg, D. P., Oas, T. G., Enhanced protein flexibility caused by a destabilizing amino acid replacement in BPTI (1997) J. Mol. Biol., 269, pp. 154-164
Viles, J. H., Duggan, B. M., Zaborowski, E., Schwarzinger, S., Huntley, J. J. A., Kroon, G. J. A., Dyson, H. J., Potential bias in NMR relaxation data introduced by peak intensity analysis and curve fitting methods (2001) J. Biomol. NMR, 21, pp. 1-9
Lee, L. K., Rance, M., Chazin, W. J., Palmer, A. G., Rotational diffusion anisotropy of proteins from simultaneous analysis of 15N and 13C nuclear spin relaxation (1997) J. Biomol. NMR, 9, pp. 287-298
Br schweiler, R., Liao, X., Wright, P. E., Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling (1995) Science, 268, pp. 886-889
Clore, G. M., Driscoll, P. C., Wingfield, P. T., Gronenborn, A. M., Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse detected heteronuclear 15N-1N NMR spectroscopy (1990) Biochemistry, 29, pp. 7387-7401
Mandel, A. M., Akke, M., Palmer, A. G., Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme (1995) J. Mol. Biol., 246, pp. 144-163
Clore, G. M., Szabo, A., Bax, A., Kay, L. E., Driscoll, P. C., Gronenborn, A. M., Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins (1990) J. Am. Chem. Soc., 112, pp. 4989-4991
Palmer, A. G., Rance, M., Wright, P. E., Intramolecular motions of a zinc finger DNA-binding domain from xfin characterized by proton-detected natural abundance 13C heteronuclear NMR spectroscopy (1991) J. Am. Chem. Soc., 113, pp. 4371-4380
Herrmann, T., G ntert, P., W thrich, K., Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA (2002) J. Mol. Biol., 319, pp. 209-227
Luginb hl, P., G ntert, P., Billeter, M., W thrich, K., The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules (1996) J. Biomol. NMR, 8, pp. 136-146
Laskowski, R. A., Rullmann, J. A., MacArthur, M. W., Kaptein, R., Thornton, J. M., AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR (1996) J. Biomol. NMR, 8, pp. 477-486
G ntert, P., Mumenthaler, C., W thrich, K., Torsion angle dynamics for NMR structure calculation with the new program DYANA (1997) J. Mol. Biol., 273, pp. 283-298
Martin, J. L., Thioredoxin a fold for all reasons (1995) Structure, 15, pp. 245-250
Kay, L. E., Torchia, D. A., Bax, A., Backbone dynamics of proteins as studied by nitrogen-15 inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease (1989) Biochemistry, 28, pp. 8972-8979
Landry, S. J., Steede, N. K., Maskos, K., Temperature dependence of backbone dynamics in loops of human mitochondrial heat shock protein 10 (1997) Biochemistry, 36, pp. 10975-10986
Even s, J., Fors n, S., Malmendal, A., Akke, M., Backbone dynamics and energetics of a calmodulin domain mutant exchanging between closed and open conformations (1999) J. Mol. Biol., 289, pp. 603-617
Seewald, M. J., Pichumani, K., Stowell, C., Tibbals, B. V., Regan, L., Stone, M. J., The role of backbone conformational heat capacity in protein stability: Temperature-dependent dynamics of the B1 domain of Streptococcal protein G (2000) Protein Sci., 9, pp. 1177-1193
Lee, A. L., Sharp, K. A., Kranza, J. K., Song, X., Wand, A. J., Temperature dependence of the internal dynamics of a calmodulin-peptide complex (2002) Biochemistry, 41, pp. 13814-13825
Kovrigin, E. L., Cole, R., Loria, J. P., Temperature dependence of the backbone dynamics of Ribonuclease A in the ground state and bound to the inhibitor 5 -phosphorhymidine (3 -5) pyrophosphatase adenosine 3 -phosphate (2003) Biochemistry, 42, pp. 5279-5291
Meekhof, A. E., Freund, S. M., Probing residual structure and backbone dynamics on the milli- to picosecond time scale in a urea-denatured fibronectin type III domain (1999) J. Mol. Biol., 86, pp. 579-592
Stone, M. J., NMR relaxation studies of the role of conformational entropy in stability and ligand binding (2001) Acc. Chem. Res., 34, pp. 379-388
Wintrode, P. L., Zhang, D., Vaidehi, N., Arnold, F. H., Goddard III, W. A., Protein dynamics in a family of laboratory evolved thermophilic enzymes (2003) J. Mol. Biol., 327, pp. 745-757
Georgescu, R. E., Garcia-Mira, M. M., Tasayco, M. L., Sanchez-Ruiz, J. M., Heat capacity analysis of oxidized Escherichia coli thioredoxin fragments (1-73, 74-108) and their noncovalent complex. Evidence for the burial of apolar surface in protein unfolded states (2001) Eur. J. Biochem., 268, pp. 1477-1485
Solution structure and backbone dynamics of the K18G/R82E Alicyclobacillus acidocaldarius thioredoxin mutant: A molecular analysis of its reduced thermal stability
No general strategy for thermostability has been yet established, because the extra stability of thermophiles appears to be the sum of different cumulative stabilizing interactions. In addition, the increase of conformational rigidity observed in many thermophilic proteins, which in some cases disappears when mesophilic and thermophilic proteins are compared at their respective physiological temperatures, suggests that evolutionary adaptation tends to maintain corresponding states with respect to conformational flexibility. In this study, we accomplished a structural analysis of the K18G/R82E Alicyclobacillus acidocaldarius thioredoxin (BacTrx) mutant, which has reduced heat resistance with respect to the thermostable wildtype. Furthermore, we have also achieved a detailed study, carried out at 25, 45, and 65 degreesC, of the backbone dynamics of both the BacTrx and its K18G/R82E mutant. Our findings clearly indicate that the insertion of the two mutations causes a loss of energetically favorable long-range interactions and renders the secondary structure elements of the double mutants more similar to those of the mesophilic Escherichia coli thioredoxin. Moreover, protein dynamics analysis shows that at room temperature the BacTrx, as well as the double mutant, are globally as rigid as the mesophilic thioredoxins; differently, at 65 degreesC, which is in the optimal growth temperature range of A. acidocaldarius, the wild-type retains its rigidity while the double mutant is characterized by a large increase of the amplitude of the internal motions. Finally, our research interestingly shows that fast motions on the pico- to nanosecond time scale are not detrimental to protein stability and provide an entropic stabilization of the native state. This study further confirms that protein thermostability is reached through diverse stabilizing interactions, which have the key role to maintain the structural folding stable and functional at the working temperature.
Solution structure and backbone dynamics of the K18G/R82E Alicyclobacillus acidocaldarius thioredoxin mutant: A molecular analysis of its reduced thermal stability
Solution structure and backbone dynamics of the K18G/R82E Alicyclobacillus acidocaldarius thioredoxin mutant: A molecular analysis of its reduced thermal stability
Kim YH, Shin SW, Pellicano R, Fagoonee S, Choi IJ, Kim YI, Park B, Choi JM, Kim SG, Choi J, Park JY, Oh S, Yang HJ, Lim JH, Im JP, Kim JS, Jung HC, Ponzetto A, Figura N, Malfertheiner P, Choi IJ, Kook MC, Kim YI, Cho SJ, Lee JY, Kim CG, Park B, Nam BH, Bae SE, Choi KD, Choe J, Kim SO, Na HK, Choi JY, Ahn JY, Jung KW, Lee J, Kim DH, Chang HS, Song HJ, Lee GH, Jung HY, Seta T, Takahashi Y, Noguchi Y, Shikata S, Sakai T, Sakai K, Yamashita Y, Nakayama T, Leja M, Park JY, Murillo R, Liepniece-karele I, Isajevs S, Kikuste I, Rudzite D, Krike P, Parshutin S, Polaka I, Kirsners A, Santare D, Folkmanis V, Daugule I, Plummer M, Herrero R, Tsukamoto T, Nakagawa M, Kiriyama Y, Toyoda T, Cao X, Corral JE, Mera R, Dye CW, Morgan DR, Lee YC, Lin JT, Garcia Martin R, Matia Cubillo A, Lee SH, Park JM, Han YM, Ko WJ, Hahm KB, Leontiadis GI, Ford AC, Ichinose M, Sugano K, Jeong M, Park JM, Han YM, Park KY, Lee DH, Yoo JH, Cho JY, Hahm KB, Bang CS, Baik GH, Shin IS, Kim JB, Suk KT, Yoon JH, Kim YS, Kim DJ * Helicobacter pylori Eradication for Prevention of Metachronous Recurrence after Endoscopic Resection of Early Gastric Cancer(297 views) N Engl J Med (ISSN: 0028-4793, 0028-4793linking, 1533-4406electronic), 2015 Jun; 30642104201566393291: 749-756. Impact Factor:59.558 ViewExport to BibTeXExport to EndNote