Format

Send to

Choose Destination
FEBS Lett. 2007 Aug 21;581(21):3996-4000. Epub 2007 Jul 25.

Crystal structure of the flavoprotein ArsH from Sinorhizobium meliloti.

Author information

1
Department of Biochemistry and Molecular Biology, Wayne State University, School of Medicine, 540 East Canfield Avenue, Detroit, MI 48201, USA.

Abstract

Purified 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.

PMID:
17673204
PMCID:
PMC1989112
DOI:
10.1016/j.febslet.2007.07.039
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Wiley Icon for PubMed Central
Loading ...
Support Center