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Protein Science (2007), 16:2483-2490. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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Crystal structure of an apo form of Shigella flexneri ArsH protein with an NADPH-dependent FMN reductase activity

Ivan I. Vorontsov1, George Minasov1, Joseph S. Brunzelle2, Ludmilla Shuvalova1, Olga Kiryukhina1, Frank R. Collart3, and Wayne F. Anderson1

1 Department of Molecular Pharmacology and Biological Chemistry, Northwestern University, Feinberg School of Medicine, Chicago, Illinois 60611, USA
2 Life Science Collaborative Access Team, Advanced Photon Source, Argonne National Laboratory, Argonne, Illinois 60439, USA
3 Biosciences Division, Argonne National Laboratory, Argonne, Illinois 60439, USA

(RECEIVED May 27, 2007; FINAL REVISION August 7, 2007; ACCEPTED August 10, 2007)

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 Å 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.

Keywords: crystal structure; flavin binding; arsenic resistance; ArsH; NADPH-dependant FMN reductase


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