1YVS

Trimeric domain swapped barnase

Summary for 1YVS

• Entry DOI: 10.2210/pdb1yvs/pdb
• Descriptor: BARNASE, SULFATE ION (3 entities in total)
• Functional Keywords: endonuclease, ribonuclease, domain swapped, trimer
• Biological source: Bacillus amyloliquefaciens
• Cellular location: Secreted: P00648
• Total number of polymer chains: 1
• Total formula weight: 12590.85

Authors

Zegers, I.,Wyns, L. (deposition date: 1998-12-10, release date: 1999-02-02, Last modification date: 2024-05-22)

Primary citation

Zegers, I.,Deswarte, J.,Wyns, L.
Trimeric domain-swapped barnase.
Proc.Natl.Acad.Sci.USA, 96:818-822, 1999

PubMed Abstract: 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.

PubMed: 9927651
DOI: 10.1073/pnas.96.3.818

Experimental method

X-RAY DIFFRACTION (2.2 Å)