1yvs: Difference between revisions
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{{STRUCTURE_1yvs| PDB=1yvs | SCENE= }} | |||
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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.]] | ||
[[Category: | [[Category: Domain swapped]] | ||
[[Category: | [[Category: Endonuclease]] | ||
[[Category: | [[Category: Ribonuclease]] | ||
[[Category: | [[Category: Trimer]] | ||
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Revision as of 16:51, 3 May 2008
TRIMERIC DOMAIN SWAPPED BARNASE
OverviewOverview
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 StructureAbout this Structure
1YVS is a Single protein structure of sequence from Bacillus amyloliquefaciens. Full crystallographic information is available from OCA.
ReferenceReference
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