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1yvs
From Proteopedia
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| , resolution 2.2Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 15:28:08 2008
