1yvs
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1yvs.jpg|left|200px]] | + | [[Image:1yvs.jpg|left|200px]] |
| - | + | ||
| - | '''TRIMERIC DOMAIN SWAPPED BARNASE''' | + | {{Structure |
| + | |PDB= 1yvs |SIZE=350|CAPTION= <scene name='initialview01'>1yvs</scene>, resolution 2.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''TRIMERIC DOMAIN SWAPPED BARNASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1YVS is a [ | + | 1YVS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YVS OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9927651 9927651] |
[[Category: Bacillus amyloliquefaciens]] | [[Category: Bacillus amyloliquefaciens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 21: | Line 30: | ||
[[Category: trimer]] | [[Category: trimer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:28:08 2008'' |
Revision as of 13:28, 20 March 2008
| |||||||
| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| 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
