1yvs
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(New page: 200px<br /><applet load="1yvs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yvs, resolution 2.2Å" /> '''TRIMERIC DOMAIN SWAPP...)
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Revision as of 04:58, 21 November 2007
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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 with SO4 as ligand. 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
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