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Crystal structure of the flavoprotein ArsH from Sinorhizobium meliloti.


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.

SUBMITTER: Ye J 

PROVIDER: S-EPMC1989112 | biostudies-literature | 2007 Aug

REPOSITORIES: biostudies-literature

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Crystal structure of the flavoprotein ArsH from Sinorhizobium meliloti.

Ye Jun J   Yang Hung-Chi HC   Rosen Barry P BP   Bhattacharjee Hiranmoy H  

FEBS letters 20070725 21


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  ...[more]

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