Crystal structure of the flavoprotein ArsH from Sinorhizobium meliloti
Crystal structure of the flavoprotein ArsH from Sinorhizobium meliloti
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DOI：
10.1016/j.febslet.2007.07.039
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发表时间：
2007-08-21
期刊：
影响因子：
3.5
通讯作者：
Bhattacharjee, Hirannioy
中科院分区：
文献类型：
--
作者：
Ye, Jun;Yang, Hung-Chi;Bhattacharjee, Hirannioy
从苜蓿中华根瘤菌中纯化的ArsH表现出NADPH：FMN依赖性的分子O-2还原为过氧化氢，并催化偶氮染料的还原。在1.8埃分辨率下测定了ArsH的结构。ArsH在不对称单元中以八个分子结晶，形成两个四聚体。每个单体都有一个核心结构域，中心有一个五链平行的P-折叠，两个单体相互作用形成一个经典的黄素氧还蛋白样二聚体。ArsH的N-和C-末端延伸参与亚基之间的相互作用和四聚体的形成。该结构可以提供洞察ArsH如何参与砷解毒。(c)2007年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
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 angstrom 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 P-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. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.