Structural and binding properties of the PASTA domain of PonA2, a key penicillin binding protein from Mycobacterium tuberculosis(475 views) Calvanese L, Falcigno L, Maglione C, Marasco D, Ruggiero A, Squeglia F, Berisio R, D'Auria G
Keywords: Binding, Structure, Tuberculosis, Antibiotics, Polymers, Proteins, Structure (composition), Antibiotic Binding, Binding Properties, Mycobacterium Tuberculosis, Penicillin-Binding Proteins, Solution Structures, Structural Similarity, Binding Energy, Beta Lactam, Penicillin Binding Protein, Peptidoglycan, Pona2 Protein, Unclassified Drug, Alpha Helix, Article, Carboxy Terminal Sequence, Centrifugation, Complex Formation, Controlled Study, Dormancy, Enzyme Active Site, Heteronuclear Nuclear Magnetic Resonance, Heteronuclear Single Quantum Coherence, Isothermal Titration Calorimetry, Ligand Binding, Nonhuman, Nuclear Overhauser Effect, Pasta Domain, Protein Binding, Protein Conformation, Protein Domain, Protein Expression, Protein Secondary Structure, Sequence Analysis, Surface Plasmon Resonance, Surface Property,
Affiliations: *** IBB - CNR ***
CIRPeB, University of Naples Federico II, Naples, Italy
Department of Pharmacy, University of Naples Federico II, via Mezzocannone 16, 80134 Naples, Italy
Institute of Biostructures and Bioimaging-CNR, via Mezzocannone 16, 80134 Naples, Italy
Department of Chemical Sciences, University of Naples Federico II, via Cintia 45, 80126 Naples, Italy
References: Morandi, M., Sali, M., Manganelli, R., Delogu, G., (2013) J Infect Dev Ctries, 7, pp. 169-18
Ruggiero, A., Marchant, J., Squeglia, F., Makarov, V., De Simone, A., Berisio, R., (2013) J Biomol Struct Dyn, 31, pp. 195-205
Ruggiero, A., De Simone, P., Smaldone, G., Squeglia, F., Berisio, R., (2012) Curr Protein Pept Sci, 13, pp. 756-766
Ruggiero, A., Marasco, D., Squeglia, F., Soldini, S., Pedone, E., Pedone, C., Berisio, R., (2010) Structure, 18, pp. 1184-1190
Ruggiero, A., Tizzano, B., Pedone, E., Pedone, C., Wilmanns, M., Berisio, R., (2009) J Mol Biol, 385, pp. 153-162
Correale, S., Ruggiero, A., Capparelli, R., Pedone, E., Berisio, R., (2013) Acta Crystallogr D Biol Crystallogr, 69, pp. 1697-1706
Sauvage, E., Kerff, F., Terrak, M., Ayala, J. A., Charlier, P., (2008) FEMS Microbiol Rev, 32, pp. 234-258
Mukamolova, G. V., Turapov, O. A., Young, D. I., Kaprelyants, A. S., Kell, D. B., Young, M., (2002) Mol Microbiol, 46, pp. 623-635
Van Gunsteren, W. F., Berendsen, H. J., Hermans, J., Hol, W. G., Postma, J. P., (1983) Proc Natl Acad Sci USA, 80, pp. 4315-4319
Chao, M. C., Kieser, K. J., Minami, S., Mavrici, D., Aldridge, B. B., Fortune, S. M., Alber, T., Rubin, E., (2013) J. PLOS Pathogens, 9, pp. e1003197
Chao, M. C., Rubin, E., (2010) J. Annu Rev Microbiol, 64, pp. 293-311
Sung, M. T., Lai, Y. T., Huang, C. Y., Chou, L. Y., Shih, H. W., Cheng, W. C., Wong, C. H., Ma, C., (2009) Proc Natl Acad Sci USA, 106, pp. 8824-8829
Dessen, A., Mouz, N., Gordon, E., Hopkins, J., Dideberg, O., (2001) J Biol Chem, 276, pp. 45106-45112
Yeats, C., Finn, R. D., Bateman, A., (2002) Trends Biochem Sci, 27, p. 438
Shah, I. M., Laaberki, M. H., Popham, D. L., Dworkin, (2008) J. Cell, 135, pp. 486-496
Squeglia, F., Marchetti, R., Ruggiero, A., Lanzetta, R., Marasco, D., Dworkin, J., Petoukhov, M., Silipo, A., (2011) J Am Chem Soc, 133, pp. 20676-20679
Mir, M., Asong, J., Li, X., Cardot, J., Boons, G. J., Husson, R. N., (2011) PLOS Pathogens, 7, pp. e1002182
Maestro, B., Novakova, L., Hesek, D., Lee, M., Leyva, E., Mobashery, S., Sanz, J. M., Branny, P., (2011) FEBS Lett, 585, pp. 357-363
Vandal, O. H., Pierini, L. M., Schnappinger, D., Nathan, C. F., Ehrt, S., (2008) Nat Med, 14, pp. 849-854
Patru, M. M., Pavelka, Jr. M. S., (2010) J Bacteriol, 192, pp. 3043-3054
Ruggiero, A., Squeglia, F., Marasco, D., Marchetti, R., Molinaro, A., Berisio, R., (2011) Biochem J, 435, pp. 33-41
Gordon, E., Mouz, N., Duee, E., Dideberg, O., (2000) J Mol Biol, 299, pp. 477-485
Hildebrand, A., Remmert, M., Biegert, A., Soding, (2009) J. Proteins, 77 (SUPPL. 9), pp. 128-132
Mathur, A., Shankaracharya, Vidyarthi, A. S., (2012) J Mol Model, 18, pp. 3021-3023
Cheng, T. J., Sung, M. T., Liao, H. Y., Chang, Y. F., Chen, C. W., Huang, C. Y., Chou, L. Y., Cheng, W. C., (2008) Proc Natl Acad Sci USA, 105, pp. 431-436
Hett, E. C., Chao, M. C., Steyn, A. J., Fortune, S. M., Deng, L. L., Rubin, E., (2007) J. Mol Microbiol, 66, pp. 658-668
Rodriguez, R., Chinea, G., Lopez, N., Pons, T., Vriend, G., (1998) Bioinformatics, 14, pp. 523-528
Koradi, R., Billeter, M., Wuthrich, K., (1996) J Mol Graph, 14, pp. 51-55. , 29-32
Poletto, M., Vascotto, C., Scognamiglio, P. L., Lirussi, L., Marasco, D., Tell, G., (2013) Biochem J, 452, pp. 545-557
Structural and binding properties of the PASTA domain of PonA2, a key penicillin binding protein from Mycobacterium tuberculosis
PonA2 is one of the two class A penicillin binding proteins of Mycobacterium tuberculosis, the etiologic agent of tuberculosis. It plays a complex role in mycobacterial physiology and is spotted as a promising target for inhibitors. PonA2 is involved in adaptation of M. tuberculosis to dormancy, an ability which has been attributed to the presence in its sequence of a C-terminal PASTA domain. Since PASTA modules are typically considered as beta-lactam antibiotic binding domains, we determined the solution structure of the PASTA domain from PonA2 and analyzed its binding properties versus a plethora of potential binders, including the beta-lactam antibiotics, two typical muropeptide mimics, and polymeric peptidoglycan. We show that, despite a high structural similarity with other PASTA domains, the PASTA domain of PonA2 displays different binding properties, as it is not able to bind muropeptides, or beta-lactams, or polymeric peptidoglycan. These results indicate that the role of PASTA domains cannot be generalized, as their specific binding properties strongly depend on surface residues, which are widely variable. (c) 2013 Wiley Periodicals, Inc. Biopolymers 101: 712-719, 2014.
Structural and binding properties of the PASTA domain of PonA2, a key penicillin binding protein from Mycobacterium tuberculosis