1yvs

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Trimeric 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.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:SO4
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RNBR_BACAM Hydrolyzes phosphodiester bonds in RNA, poly- and oligoribonucleotides resulting in 3'-nucleoside monophosphates via 2',3'-cyclophosphate intermediates.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
7 reviews cite this structure
3D domain swapping: as domains continue to swap.
Liu et al. (2002)
6 more
22 other articles
No citations found

See Also

References

  1. ↑ Zegers I, Deswarte J, Wyns L. Trimeric domain-swapped barnase. Proc Natl Acad Sci U S A. 1999 Feb 2;96(3):818-22. PMID:9927651

Contents


PDB ID 1yvs

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