1yvs

Trimeric domain swapped barnaseTrimeric domain swapped barnase

Structural highlights 1yvs is a 1 chain structure with sequence from Bacillus amyloliquefaciens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Barnase Ribonuclease

spinqualitylabelsall models 1yvs, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image