Binding of a substrate analog to a domain swapping protein: X-ray structure of the complex of bovine seminal ribonuclease with uridylyl(2 ', 5 ')adenosine
Binding of a substrate analog to a domain swapping protein: X-ray structure of the complex of bovine seminal ribonuclease with uridylyl(2 ', 5 ')adenosine(425 views) Vitagliano L, Adinolfi S, Riccio A, Sica F, Zagari A, Mazzarella L
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 1998 Sep; 7(8): 1691-1699.
Affiliations: Centro di Studio di Biocristallografia, Dipartimento di Chimica, Università degli Studi di Napoli Federico II, Via Mezzocannone 4, I-80134 Napoli, Italy
Istituto di Biochimica delle Proteine ed Enzimologia, CNR, via Marconi, 10, I-80125 Napoli, Italy
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Laccetti, P., Spalletti-Cemia, D., Portella, G., De Corato, P., D'Alessio, G., Vecchio, G., Seminal ribonuclease inhibits tumor growth and reduces the metastatic potential of Lewis carcinoma (1994) Cancer Res, 54, pp. 4253-4256
Laskowski, R.A., MacArthur, M.W., Moss, D.S., Thorton, J.M., PROCHECK: A program to check the stereochemical quality of protein structure (1993) J Appl Crystallogr, 26, pp. 283-291
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Piccoli, R., Tamburrini, M., Piccialli, G., Di Donato, A., Parente, A., D'Alessio, G., The dual-mode quaternary structure of seminal RNase (1992) Proc Natl Acad Sci USA, 89, pp. 1870-1874
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Aguilar, C. F., Thomas, P. J., Mills, A., Moss, D. S., Palmer, R. A., Newly observed binding mode in pancreatic ribonuclease (1992) J Mol Biol, 224, pp. 2665-2676
Gilliland, G. L., Dill, J., Pechik, L., Svensson, L. A., Sjolin, L., The active site of bovine pancreatic ribonuclease: An example of solvent modulated specificity (1994) Protein Pept Lett, 1, pp. 60-65
Hendrickson, W. A., Stereochemically restained refinement of macromolecular structures (1985) Methods Enzymol, 115, pp. 252-270
Jones, T. A., A graphics model building and refinement system for macromolecules (1978) J Appl Crystallogr, 11, pp. 268-272
Jones, T. A., Zou, J. -Y., Cowan, S. W., Kjeldgaard, M., Improved methods for building protein models in electron-density maps and the location of errors in these models (1991) Acta Crystallogr, A47, pp. 110-119
Kraulis, P. J., MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures (1991) J Appl Crystallogr, 24, pp. 946-950
Laskowski, R. A., MacArthur, M. W., Moss, D. S., Thorton, J. M., PROCHECK: A program to check the stereochemical quality of protein structure (1993) J Appl Crystallogr, 26, pp. 283-291
Lisgarten, J. N., Maes, D., Wyns, L., Aguilar, C. F., Palmer, R., Structure of the crystalline complex of deoxycytidylyl-3, 5 -guanosine (3, 5 -dCpdG) cocrystallized with ribonuclease at 1. 9 resolution (1995) Acta Crystallogr D, 51, pp. 767-771
Moodie, S. L., Thornton, J. M., A study into the effects of protein binding on nucleotide conformation (1993) Nucl Acid Res, 21, pp. 1369-1380
Pavlovsky, A. G., Borisova, S. N., Borisov, V. V., Antonov, I. V., Karpeisky, M. Y., The structure of the complex of ribonuclease S with fluoride analogue of UpA at 2. 5 resolution (1978) FEBS Lett, 92, pp. 258-262
Radha Kishan, K. V., Chandra, N. R., Sudarsanakumar, C., Suguna, K., Vuayan, M., Water-dependent domain motion and flexibility in ribonuclease A and the invariant features in its hydration shell. An X-ray study of two low-humidity crystal forms of the enzyme (1995) Acta Crystallogr, D51, pp. 703-710
Richards, F. M., Wyckoff, H. W., Ribonuclease S (1973) Atlas of Molecular Structures in Biology, 1. , Philips DC, Richards FM, eds. Oxford, UK: Claderon
Binding of a substrate analog to a domain swapping protein: X-ray structure of the complex of bovine seminal ribonuclease with uridylyl(2 ', 5 ')adenosine
Bovine seminal ribonuclease (BS-RNase) is a unique member of the pancreatic-like ribonuclease superfamily. The native enzyme is a mixture of two dimeric forms with distinct structural features. The most abundant form is characterized by the swapping of N-terminal fragments. In this paper, the crystal structure of the complex between the swapping dimer and uridylyl(2'5')adenosine is reported at 2.06 Angstrom resolution. The refined model has a crystallographic R-factor of 0.184 and good stereochemistry. The quality of the electron density maps enables the structure of both the inhibitor and active site residues to be unambiguously determined. The overall architecture of the active site is similar to that of RNase A. The dinucleotide adopts an extended conformation with the pyrimidine and purine base interacting with Thr45 and Asn71, respectively. Several residues (Gln11, His12, Lys41, His 119, and Phe 120) bind the oxygens of the phosphate group. The structural similarity of the active sites of BS-RNase and RNase A includes some specific water molecules believed to be relevant to catalytic activity. Upon binding of the dinucleotide, small but significant modifications of the tertiary and quaternary structure of the protein are observed. The ensuing correlation of these modifications with the catalytic activity of the enzyme is discussed.
Binding of a substrate analog to a domain swapping protein: X-ray structure of the complex of bovine seminal ribonuclease with uridylyl(2 ', 5 ')adenosine
No results.
Binding of a substrate analog to a domain swapping protein: X-ray structure of the complex of bovine seminal ribonuclease with uridylyl(2 ', 5 ')adenosine