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1yvs

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[[Image:1yvs.jpg|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yvs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yvs OCA], [http://www.ebi.ac.uk/pdbsum/1yvs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yvs RCSB]</span>
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'''TRIMERIC DOMAIN SWAPPED BARNASE'''
'''TRIMERIC DOMAIN SWAPPED BARNASE'''
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[[Category: Wyns, L.]]
[[Category: Wyns, L.]]
[[Category: Zegers, I.]]
[[Category: Zegers, I.]]
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[[Category: domain swapped]]
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[[Category: Domain swapped]]
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[[Category: endonuclease]]
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[[Category: Endonuclease]]
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[[Category: ribonuclease]]
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[[Category: Ribonuclease]]
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[[Category: trimer]]
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[[Category: Trimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:51:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:24:26 2008''
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Revision as of 13:51, 3 May 2008

Image:1yvs.jpg

Template:STRUCTURE 1yvs

TRIMERIC DOMAIN SWAPPED BARNASE


Overview

The structure of a trimeric domain-swapped form of barnase (EC 3.1. 27.3) was determined by x-ray crystallography at a resolution of 2.2 A from crystals of space group R32. Residues 1-36 of one molecule associate with residues 41-110 from another molecule related through threefold symmetry. The resulting cyclic trimer contains three protein folds that are very similar to those in monomeric barnase. Both swapped domains contain a nucleation site for folding. The formation of a domain-swapped trimer is consistent with the description of the folding process of monomeric barnase as the formation and subsequent association of two foldons.

About this Structure

1YVS is a Single protein structure of sequence from Bacillus amyloliquefaciens. Full crystallographic information is available from OCA.

Reference

Trimeric domain-swapped barnase., Zegers I, Deswarte J, Wyns L, Proc Natl Acad Sci U S A. 1999 Feb 2;96(3):818-22. PMID:9927651 Page seeded by OCA on Sat May 3 16:51:19 2008

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