2FZV

Crystal Structure of an apo form of a Flavin-binding Protein from Shigella flexneri

Summary for 2FZV

• Entry DOI: 10.2210/pdb2fzv/pdb
• Descriptor: putative arsenical resistance protein, CALCIUM ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: flavin binding protein, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, unknown function
• Biological source: Shigella flexneri 2a
• Total number of polymer chains: 4
• Total formula weight: 124828.10

Authors

Vorontsov, I.I.,Minasov, G.,Brunzelle, J.S.,Shuvalova, L.,Collart, F.R.,Joachimiak, A.,Anderson, W.F.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2006-02-10, release date: 2006-02-21, Last modification date: 2024-02-14)

Primary citation

Vorontsov, I.I.,Minasov, G.,Brunzelle, J.S.,Shuvalova, L.,Kiryukhina, O.,Collart, F.R.,Anderson, W.F.
Crystal structure of an apo form of Shigella flexneri ArsH protein with an NADPH-dependent FMN reductase activity
Protein Sci., 16:2483-2490, 2007

PubMed Abstract: The arsH gene or its homologs are a frequent part of the arsenic resistance system in bacteria and eukaryotes. Although a specific biological function of the gene product is unknown, the ArsH protein was annotated as a member of the NADPH-dependent FMN reductase family based on a conserved (T/S)XRXXSX(T/S) fingerprint motif common for FMN binding proteins. Presented here are the first crystal structure of an ArsH protein from Shigella flexneri refined at 1.7 A resolution and results of enzymatic activity assays that revealed a strong NADPH-dependent FMN reductase and low azoreductase activities. The ArsH apo protein has an alpha/beta/alpha-fold typical for FMN binding proteins. The asymmetric unit consists of four monomers, which form a tetramer. Buried surface analysis suggests that this tetramer is likely to be the relevant biological assembly. Dynamic light scattering experiments are consistent with this hypothesis and show that ArsH in solution at room temperature does exist predominantly in the tetrameric form.

PubMed: 17962405
DOI: 10.1110/ps.073029607

Experimental method

X-RAY DIFFRACTION (1.7 Å)