ArticleJournal of bacteriology2007
Crystal structure of the NADH:quinone oxidoreductase WrbA from Escherichia coli.
Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- A roadmap to chemically reactive species: how diverse oxidants affectMicrobiology and molecular biology reviews : MMBR · 2025Review
- Exploring the genome-wide transcriptomic responses of Bulinus truncatus to Schistosoma haematobium infection: An important host-parasite system involved in the transmission of human urogenital schistosomiasis.Molecular immunology · 2024Article
- Characterization of phage vB_EcoS-EE09 infectingMicroorganisms · 2023Article
- Differential Roles of a Family of Flavodoxin-Like Proteins That Promote Resistance to Quinone-Mediated Oxidative Stress in Candida albicans.Infection and immunity · 2021Article
- An aspartyl protease-mediated cleavage regulates structure and function of a flavodoxin-like protein and aids oxidative stress survival.PLoS pathogens · 2021Article
- Steric hindrance controls pyridine nucleotide specificity of a flavin-dependent NADH:quinone oxidoreductase.Protein science : a publication of the Protein Society · 2019Article
- Evolutionary Relationships Between Low Potential Ferredoxin and Flavodoxin Electron Carriers.Frontiers in energy research · 2019Article
- WrpA Is an Atypical Flavodoxin Family Protein under Regulatory Control of the Brucella abortus General Stress Response System.Journal of bacteriology · 2016Article
- Flavodoxin-Like Proteins Protect Candida albicans from Oxidative Stress and Promote Virulence.PLoS pathogens · 2015Article
- Unravelling the Structural and Molecular Basis Responsible for the Anti-Biofilm Activity of Zosteric Acid.PloS one · 2015Article
- Pseudomonas aeruginosa MdaB and WrbA are water-soluble two-electron quinone oxidoreductases with the potential to defend against oxidative stress.Journal of microbiology (Seoul, Korea) · 2014Article
- Proteomic profiling of Rhizobium tropici PRF 81: identification of conserved and specific responses to heat stress.BMC microbiology · 2012Article
- Biphasic kinetic behavior of E. coli WrbA, an FMN-dependent NAD(P)H:quinone oxidoreductase.PloS one · 2012Article
- Structure determination and functional analysis of a chromate reductase from Gluconacetobacter hansenii.PloS one · 2012Article
- KefF, the regulatory subunit of the potassium efflux system KefC, shows quinone oxidoreductase activity.Journal of bacteriology · 2011Article
- Genome-wide functional profiling reveals genes required for tolerance to benzene metabolites in yeast.PloS one · 2011Article
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- Compensations for diminished terminal oxidase activity in Escherichia coli: cytochrome bd-II-mediated respiration and glutamate metabolism.The Journal of biological chemistry · 2010Article
- Identification of Escherichia coli HemG as a novel, menadione-dependent flavodoxin with protoporphyrinogen oxidase activity.Biochemistry · 2009Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The flavoprotein WrbA, originally described as a tryptophan (W) repressor-binding protein in Escherichia coli, has recently been shown to exhibit the enzymatic activity of a NADH:quinone oxidoreductase. This finding points toward a possible role in stress response and in the maintenance of a supply of reduced quinone. We have determined the three-dimensional structure of the WrbA holoprotein from E. coli at high resolution (1.66 A), and we observed a characteristic, tetrameric quaternary structure highly similar to the one found in the WrbA homologs of Deinococcus radiodurans and Pseudomonas aeruginosa. A similar tetramer was originally observed in an iron-sulfur flavoprotein involved in the reduction of reactive oxygen species. Together with other, recently characterized proteins such as YhdA or YLR011wp (Lot6p), these tetrameric flavoproteins may constitute a large family with diverse functions in redox catalysis. WrbA binds substrates at an active site that provides an ideal stacking environment for aromatic moieties, while providing a pocket that is structured to stabilize the ADP part of an NADH molecule in its immediate vicinity. Structures of WrbA in complex with benzoquinone and NADH suggest a sequential binding mechanism for both molecules in the catalytic cycle.
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