| pubmed-article:17951395 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17951395 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:17951395 | lifeskim:mentions | umls-concept:C0027280 | lld:lifeskim |
| pubmed-article:17951395 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:17951395 | lifeskim:mentions | umls-concept:C1136197 | lld:lifeskim |
| pubmed-article:17951395 | lifeskim:mentions | umls-concept:C1413742 | lld:lifeskim |
| pubmed-article:17951395 | lifeskim:mentions | umls-concept:C0027289 | lld:lifeskim |
| pubmed-article:17951395 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:17951395 | pubmed:dateCreated | 2007-12-6 | lld:pubmed |
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| pubmed-article:17951395 | pubmed:abstractText | 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. | lld:pubmed |
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| pubmed-article:17951395 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:17951395 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17951395 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17951395 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:17951395 | pubmed:issn | 1098-5530 | lld:pubmed |
| pubmed-article:17951395 | pubmed:author | pubmed-author:EinsleOliverO | lld:pubmed |
| pubmed-article:17951395 | pubmed:author | pubmed-author:FerryJames... | lld:pubmed |
| pubmed-article:17951395 | pubmed:author | pubmed-author:AndradeSusana... | lld:pubmed |
| pubmed-article:17951395 | pubmed:author | pubmed-author:PatridgeEric... | lld:pubmed |
| pubmed-article:17951395 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17951395 | pubmed:volume | 189 | lld:pubmed |
| pubmed-article:17951395 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17951395 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17951395 | pubmed:pagination | 9101-7 | lld:pubmed |
| pubmed-article:17951395 | pubmed:dateRevised | 2010-9-16 | lld:pubmed |
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| pubmed-article:17951395 | pubmed:meshHeading | pubmed-meshheading:17951395... | lld:pubmed |
| pubmed-article:17951395 | pubmed:meshHeading | pubmed-meshheading:17951395... | lld:pubmed |
| pubmed-article:17951395 | pubmed:meshHeading | pubmed-meshheading:17951395... | lld:pubmed |
| pubmed-article:17951395 | pubmed:meshHeading | pubmed-meshheading:17951395... | lld:pubmed |
| pubmed-article:17951395 | pubmed:meshHeading | pubmed-meshheading:17951395... | lld:pubmed |
| pubmed-article:17951395 | pubmed:meshHeading | pubmed-meshheading:17951395... | lld:pubmed |
| pubmed-article:17951395 | pubmed:meshHeading | pubmed-meshheading:17951395... | lld:pubmed |
| pubmed-article:17951395 | pubmed:meshHeading | pubmed-meshheading:17951395... | lld:pubmed |
| pubmed-article:17951395 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17951395 | pubmed:articleTitle | Crystal structure of the NADH:quinone oxidoreductase WrbA from Escherichia coli. | lld:pubmed |
| pubmed-article:17951395 | pubmed:affiliation | Institute for Microbiology and Genetics, Georg August University Göttingen, Justus von Liebig Weg 11, 37077 Göttingen, Germany. susana.andrade@bio.uni-goettingen.de | lld:pubmed |
| pubmed-article:17951395 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17951395 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:947263 | entrezgene:pubmed | pubmed-article:17951395 | lld:entrezgene |
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