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Crystal structure of the flavoprotein ArsH from Sinorhizobium meliloti
Author(s) -
Ye Jun,
Yang Hung-Chi,
Rosen Barry P.,
Bhattacharjee Hiranmoy
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.07.039
Subject(s) - sinorhizobium meliloti , tetramer , chemistry , monomer , dimer , oxidoreductase , stereochemistry , crystal structure , crystallography , biochemistry , enzyme , organic chemistry , mutant , gene , polymer
Purified ArsH from Sinorhizobium meliloti exhibits NADPH:FMN‐dependent reduction of molecular O 2 to hydrogen peroxide and catalyzes reduction of azo dyes. The structure of ArsH was determined at 1.8 Å 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 β‐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.