ArticleProtein science : a publication of the Protein Society2007
Crystal structure of an apo form of Shigella flexneri ArsH protein with an NADPH-dependent FMN reductase activity.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 42 citations in OpenAlex.
- Arsenite tolerance and removal potential of the indigenous halophilic bacterium, Halomonas elongata SEK2.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2024Article
- Hybrid-genome sequence analysis of Enterobacter cloacae FACU and morphological characterization: insights into a highly arsenic-resistant strain.Functional & integrative genomics · 2024Article
- Genome-Scale Investigation of the Regulation of azoR Expression in Escherichia coli Using Computational Analysis and Transposon Mutagenesis.Microbial ecology · 2024Article
- Draft genome of Raoultella planticola, a high lead resistance bacterium from industrial wastewater.AMB Express · 2023Article
- Identification of potential light deficiency response regulators in endangered species Magnolia sinostellata.Scientific reports · 2022Article
- The ArsH Protein Product of theAntioxidants (Basel, Switzerland) · 2022Article
- Not as easy as π: An insertional residue does not explain the π-helix gain-of-function in two-component FMN reductases.Protein science : a publication of the Protein Society · 2019Article
- WrpA Is an Atypical Flavodoxin Family Protein under Regulatory Control of the Brucella abortus General Stress Response System.Journal of bacteriology · 2016Article
- Effects of Arsenite Resistance on the Growth and Functional Gene Expression of Leptospirillum ferriphilum and Acidithiobacillus thiooxidans in Pure Culture and Coculture.BioMed research international · 2015Article
- Purification, crystallization and preliminary X-ray diffraction analysis of ArsH from Synechocystis sp. strain PCC 6803.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Role of Aspergillus niger acrA in arsenic resistance and its use as the basis for an arsenic biosensor.Applied and environmental microbiology · 2012Article
- Genome of halomonas strain GFAJ-1, a blueprint for fame or business as usual.Journal of bacteriology · 2012Article
- Structure determination and functional analysis of a chromate reductase from Gluconacetobacter hansenii.PloS one · 2012Article
- Functional Promiscuity of Homologues of the Bacterial ArsA ATPases.International journal of microbiology · 2010Article
- Sequencing and expression of two arsenic resistance operons with different functions in the highly arsenic-resistant strain Ochrobactrum tritici SCII24T.BMC microbiology · 2008Article
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7 authors at 2 institutions in 1 country.
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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.
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