A potential allosteric subsite generated by domain swapping in bovine seminal ribonuclease(380 views) Vitagliano L, Adinolfi S, Sica F, Merlino A, Zagari A, Mazzarella L
Affiliations: Ctro. di Stud. di Biocristallografia, Dipartimento di Chimica, Univ.' Studi di Napoli federico II, Via Mezzocannone 4, I-80134, Napoli, Italy
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Jones, T. A., Zou, J. Y., Cowan, S. W., Kjeldgaard, M., A graphics model building and refinement system for macromolecules (1991) Acta Crystallog. Sect. a, 47, pp. 110-119
Kraulis, P. J., MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures (1991) J. Appl. Crystallog., 24, pp. 946-950
Laskowski, R. A., MacArthur, M. W., Moss, D. S., Thornton, J. M., PROCHECK-a program to check the stereochemical quality of protein structures (1993) J. Appl. Crystallog., 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 Crystallog. Sect. D, 51, pp. 767-771
Merritt, E. A., Murphy, M. E. P., Raster3D Version 2. 0- A program for photorealistic molecular graphics (1994) Acta Crystallog. Sect. D, 50, pp. 869-873
Moodie, S. L., Thornton, J. M., A study into the effects of protein binding on nucleotide conformation (1993) Nucl. Acids Res., 21, pp. 1369-1380
Opitz, J. G., Ciglic, M. I., Haugg, M., Trautwein-Fritz, K., Raillard, S. A., Jerman, T. M., Benner, S. A., Origin of the catalytic activity of bovine seminal ribonuclease against double-stranded RNA (1998) Biochemistry, 37, pp. 4023-4033
Raines, T. A., Ribonuclease A (1998) Chem. Rev., 98, pp. 1045-1066
Youle, R. J., D'Alessio, G., Antitumor RNases (1996) Ribonucleases: Structures and Functions, pp. 491-514. , G. D'Alessio, & J. F. Riordan. New York: Academic Press
A potential allosteric subsite generated by domain swapping in bovine seminal ribonuclease
Bovine seminal ribonuclease (BS-RNase) is a peculiar member of the pancreatic-like ribonuclease superfamily endowed with unique biological functions. It has been shown that native BS-RNase is a mixture of two distinct dimeric forms. The most abundant form is characterised by the swapping of the N-terminal helix. Kinetic studies have shown that this dimer is allosterically regulated, whereas the minor component, in which no swapping occurs, exhibits typical Michaelian kinetics, in order to correlate the catalytic properties with the structural features of BS-RNase, we have determined the crystal structure of the BS-RNase swapping dimer complexed with uridylyl(2'-5') guanosine. The structure of the complex was refined to an R value of 0.189 at 1.9 Angstrom resolution. Surprisingly, the enzyme binds four dinucleotide molecules, all in a non-productive way. in the two active sites, the guanine base is located in the subsite that is specific for pyrimidines. This unusual binding has been observed also in complexes of RNase A with guanine-containing nucleotides (retro-binding). One of the two additional dinucleotide molecules bound to the enzyme is located an the surface of the protein in a pocket generated by crystal packing; the second was found in a cavity at the interface between the two subunits of the swapping dimer. There are indications that the interface site plays a role in the allosteric regulation exhibited by BS-RNase. This finding suggests that domain swapping may not merely be a mechanism that proteins adopt for the transition from a monomeric to oligomeric state but can be used to achieve modulations in catalytic function. (C) 1999 Academic Press.
A potential allosteric subsite generated by domain swapping in bovine seminal ribonuclease
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A potential allosteric subsite generated by domain swapping in bovine seminal ribonuclease