2q62
From Proteopedia
(New page: 200px<br /><applet load="2q62" size="350" color="white" frame="true" align="right" spinBox="true" caption="2q62, resolution 1.800Å" /> '''Crystal Structure o...) |
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==Overview== | ==Overview== | ||
| - | Purified ArsH from Sinorhizobium meliloti exhibits NADPH:FMN-dependent | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Sinorhizobium meliloti]] | [[Category: Sinorhizobium meliloti]] | ||
[[Category: Bhattacharjee, H.]] | [[Category: Bhattacharjee, H.]] | ||
| - | [[Category: Rosen, B | + | [[Category: Rosen, B P.]] |
[[Category: Yang, H.]] | [[Category: Yang, H.]] | ||
[[Category: Ye, J.]] | [[Category: Ye, J.]] | ||
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[[Category: flavoprotein]] | [[Category: flavoprotein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:36:23 2008'' |
Revision as of 16:36, 21 February 2008
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Crystal Structure of ArsH from Sinorhizobium meliloti
Overview
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.
About this Structure
2Q62 is a Single protein structure of sequence from Sinorhizobium meliloti with as ligand. Full crystallographic information is available from OCA.
Reference
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
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