Dipartimento di Chimica, Univ. Studi Napoli Federico II, Via Cynthia, 80126 Napoli, Italy
Dipto. di Scienze Farmaceutiche, Università di Salerno, Via ponte don Melillo, 84084, Fisciano (Sa), Italy
Ist. di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 6, 80134 Napoli, Italy
References: Bennet, A.M., Choe, S., Eisenberg, D., (1994) Proc Natl Acad Sci USA, 91, pp. 3127-313
Bennet, M.J., Schlunegger, M.P., Eisenberg, D., (1995) Protein Sci, 4, pp. 2455-2468
Schlunegger, M.P., Bennet, M.J., Eisenberg, D., (1997) Advances in Protein Chemistry, pp. 61-122. , Richards, F. M., Eisenberg, D. S., Kim, P. S., Eds.
Academic Press: New York
Newcomer, M.E., (2001) Nat Struct Biol, 8, pp. 282-284
Liu, Y., Eisenberg, D., (2002) Protein Sci, 11, pp. 1285-1299
Capasso, S., Giordano, F., Mattia, C.A., Mazzarella, L., Zagari, A., (1983) Biopolymers, 22, pp. 327-332
Mazzarella, L., Capasso, S., Demasi, D., Di Lorenzo, G., Mattia, C.A., Zagari, A., (1993) Acta Cryst D, 49, pp. 389-402
Di Donato, A., Piccoli, R., D'Alessio, G., (1987) Biochem J, 241, pp. 435-440
Piccoli, R., Di Donato, A., D'Alessio, G., (1988) Biochem J, 253, pp. 329-336
Piccoli, R., Tamburini, M., Piccialli, G., Di Donato, A., Parente, A., D'Alessio, G., (1992) Proc Natl Acad Sci USA, 89, pp. 1870-1874
Berisio, R., Sica, F., Di Lorenzo, C., Di Fiore, A., Piccoli, R., Mazzarella, L., (2003) FEBS Lett, 554, pp. 105-110
Di Donato, A., Cafaro, V., Romeo, I., D'Alessio, G., (1995) Protein Sci, 4, pp. 1470-1477
Gilliland, G., (1997) Ribonucleases: Structures and Functions, pp. 306-341. , Riordan, J. F., D'Alessio, G., Eds.
Sica, F., Di Fiore, A., Zagari, A., Mazzarella, L., (2003) Proteins, 52, pp. 263-271
Zegers, I., Maes, D., Dao-Thi, M.H., Poortmans, F., Palmer, R., Wyns, L., (1994) Protein Sci, 3, pp. 2322-2339
Radha Kishan, K.V., Chandra, N.R., Sudarsanakumar, C., Suguna, K., Vijayan, M., (1995) Acta Cryst D, 51, pp. 703-710
Sadasivan, C., Nagendra, H.G., Vijayan, M., (1998) Acta Cryst D, 54, pp. 1343-1352
Merlino, A., Vitagliano, L., Ceruso, M.A., Di Nola, A., Mazzarella, L., (2002) Biopolymers, 65, pp. 274-283
Volkman, B.F., Lipson, D., Wemmer, D.E., (2001) Science, 291, pp. 2429-2433
Stock, A., (1999) Nature, 400, pp. 221-222
Feher, V.A., Cavanagh, J., (1999) Nature, 400, pp. 289-290
Nevo, R., Stroth, C., Kienberger, F., Kaftan, D., Brumfeld, V., Elbaum, M., Reich, Z., Hinterdorfer, P., (2003) Nature Struct Biol, 10, pp. 553-557
Bennet, A. M., Choe, S., Eisenberg, D., (1994) Proc Natl Acad Sci USA, 91, pp. 3127-313
Bennet, M. J., Schlunegger, M. P., Eisenberg, D., (1995) Protein Sci, 4, pp. 2455-2468
Newcomer, M. E., (2001) Nat Struct Biol, 8, pp. 282-284
Ciglic, M. I., Jackson, P. J., Raillard, S. A., Haugg, M., Jermann, T. M., Opitz, J. G., Trabesinger-Ruf, N., Benner, S. A., (1998) Biochemistry, 37, pp. 4008-4022
Opitz, J. G., Ciglic, M. I., Haugg, M., Trautwein-Fritz, K., Raillard, S. A., Jerman, T. M., Benner, S. A., (1998) Biochemistry, 37, pp. 4023-4033
Crestfield, A. M., Stein, W. H., Moore, S., (1962) Arch Biochem Biophys, (SUPPL. 1), pp. 221-222
Liu, Y., Hart, P. J., Schlunegger, M. P., Eisenberg, D., (1998) Proc Natl Acad Sci USA, 95, pp. 3437-3442
Kumar, S. M., Buyong, M., Tsai, C. J., Sinha, N., Nussinov, R., (2000) Protein Sci, 9, pp. 10-19
Ma, B., Kumar, S. M., Tsai, C. J., Nussinov, R., (1999) Protein Eng, 12, pp. 713-720
Koshland, D. E., (1958) Proc Natl Acad Sci USA, 44, pp. 98-123
Brunger, A. T., (1992) X-PLOR Version 3. 1: A System for X-Ray Crystallography and NMR, , Yale University Press, New Haven, CT
Jones, T. A., Zou, J. Y., Cowan, S. W., Kjeldgaard, M., (1991) Acta Cryst A, 47, pp. 110-119
Laskowski, R. A., MacArthur, M. W., Moss, M. D., Thornton, J. M., (1993) J Appl Crystallogr, 26, pp. 283-291
Hooft, R. W., Vriend, G., Sander, C., Abola, E. E., (1996) Nature, 381, p. 272
Campbell, R. L., Petsko, G. A., (1987) Biochemistry, 26, pp. 8579-8584
Leonidas, D. D., Shapiro, R., Irons, L. I., Russo, N., Acharya, K. R., (1997) Biochemistry, 36, pp. 5578-5588
Radha Kishan, K. V., Chandra, N. R., Sudarsanakumar, C., Suguna, K., Vijayan, M., (1995) Acta Cryst D, 51, pp. 703-710
Volkman, B. F., Lipson, D., Wemmer, D. E., (2001) Science, 291, pp. 2429-2433
Feher, V. A., Cavanagh, J., (1999) Nature, 400, pp. 289-290
Population shift vs induced fit: The case of bovine seminal ribonuclease swapping dimer
Bovine seminal ribonuclease (BS-RNase) is a unique member of the pancreatic-like ribonuclease superfamily. This enzyme exists as two conformational isomers with distinctive biological properties. The structure of the major isomer is characterized by the swapping of the N-terminal segment (M x M BS-RNase). In this article, the crystal structures of the ligand-free M x M BS-RNase and its complex with 2'-deoxycitidylyl(3',5')-2'-deoxyadenosine derived from isomorphous crystals have been refined. Interestingly, the comparison between this novel ligand-free form and the previously published sulfate-bound structure reveals significant differences. In particular, the ligand-free M x M BS-RNase is closer to the structure of M x M BS-RNase productive complexes than to the sulfate-bound form. These results reveal that M x M BS-RNase presents a remarkable flexibility, despite the structural constraints of the interchain disulfide bridges and swapping of the N-terminal helices. These findings have important implications to the ligand binding mechanism of M x M BS-RNase. Indeed, a population shift rather than a substrate-induced conformational transition may occur in the M x M BS-RNase ligand binding process. (C) 2004 Wiley Periodicals, Inc.
Population shift vs induced fit: The case of bovine seminal ribonuclease swapping dimer
No results.
Population shift vs induced fit: The case of bovine seminal ribonuclease swapping dimer