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| - | [[Image:1y92.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1y92| PDB=1y92 | SCENE= }} | | {{STRUCTURE_1y92| PDB=1y92 | SCENE= }} |
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| - | '''Crystal structure of the P19A/N67D Variant Of Bovine seminal Ribonuclease'''
| + | ===Crystal structure of the P19A/N67D Variant Of Bovine seminal Ribonuclease=== |
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| - | ==Overview==
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| - | Bovine seminal ribonuclease (BS-RNase) is a covalent homodimeric enzyme homologous to pancreatic ribonuclease (RNase A), endowed with a number of special biological functions. It is isolated as an equilibrium mixture of swapped (MxM) and unswapped (M=M) dimers. The interchanged N termini are hinged on the main bodies through the peptide 16-22, which changes conformation in the two isomers. At variance with other proteins, domain swapping in BS-RNase involves two dimers having a similar and highly constrained quaternary association, mainly dictated by two interchain disulfide bonds. This provides the opportunity to study the intrinsic ability to swap as a function of the hinge sequence, without additional effects arising from dissociation or quaternary structure modifications. Two variants, having Pro19 or the whole sequence of the hinge replaced by the corresponding residues of RNase A, show equilibrium and kinetic parameters of the swapping similar to those of the parent protein. In comparison, the x-ray structures of MxM indicate, within a substantial constancy of the quaternary association, a greater mobility of the hinge residues. The relative insensitivity of the swapping tendency to the substitutions in the hinge region, and in particular to the replacement of Pro19 by Ala, contrasts with the results obtained for other swapped proteins and can be rationalized in terms of the unique features of the seminal enzyme. Moreover, the results indirectly lend credit to the hypothesis that the major role of Pro19 resides in directing the assembly of the non-covalent dimer, the species produced by selective reduction of the interchain disulfides and considered responsible for the special biological functions of BS-RNase.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15647261}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15647261 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15647261}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Tomaselli, S.]] | | [[Category: Tomaselli, S.]] |
| | [[Category: Nuclease]] | | [[Category: Nuclease]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:01:32 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:42:49 2008'' |
Revision as of 03:42, 28 July 2008
Template:STRUCTURE 1y92
Crystal structure of the P19A/N67D Variant Of Bovine seminal Ribonuclease
Template:ABSTRACT PUBMED 15647261
About this Structure
1Y92 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
The role of the hinge loop in domain swapping. The special case of bovine seminal ribonuclease., Picone D, Di Fiore A, Ercole C, Franzese M, Sica F, Tomaselli S, Mazzarella L, J Biol Chem. 2005 Apr 8;280(14):13771-8. Epub 2005 Jan 12. PMID:15647261
Page seeded by OCA on Mon Jul 28 06:42:49 2008
