2q62 | pdb_00002q62
From Proteopedia
Crystal Structure of ArsH from Sinorhizobium meliloti
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Structural highlights
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 PubMedPurified ArsH from Sinorhizobium meliloti exhibits NADPH:FMN-dependent reduction of molecular O2 to hydrogen peroxide and catalyzes reduction of azo dyes. The structure of ArsH was determined at 1.8A resolution. ArsH crystallizes with eight molecules in the asymmetric unit forming two tetramers. Each monomer has a core domain with a central five-stranded parallel beta-sheet and two monomers interact to form a classical flavodoxin-like dimer. The N- and C-terminal extensions of ArsH are involved in interactions between subunits and tetramer formation. The structure may provide insight in how ArsH participates in arsenic detoxification. Crystal structure of the flavoprotein ArsH from Sinorhizobium meliloti.,Ye J, Yang HC, Rosen BP, Bhattacharjee H FEBS Lett. 2007 Aug 21;581(21):3996-4000. Epub 2007 Jul 25. PMID:17673204[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 08:56, 29 August 2018.