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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2007-9-25
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pubmed:abstractText |
The crystal structure of the flavodoxin-like protein WrbA with oxidized FMN bound reveals a close relationship to mammalian NAD(P)H:quinone oxidoreductase, Nqo1. Structural comparison of WrbA, flavodoxin, and Nqo1 indicates how the twisted open-sheet fold of flavodoxins is elaborated to form multimers that extend catalytic function from one-electron transfer between protein partners using FMN to two-electron reduction of xenobiotics using FAD. The structure suggests a novel physiological role for WrbA and Nqo1.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893367-11423658,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893367-11842161,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893367-14711822,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893367-16672604,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893367-16700548,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893367-178539,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893367-6782445,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893367-7530954,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893367-7568029,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893367-7756978,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893367-8516330,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893367-8637908,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893367-8780787
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0961-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2301-5
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
2007
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pubmed:articleTitle |
WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases.
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pubmed:affiliation |
Chemistry Department, Princeton University, Princeton, New Jersey 08544-1009, USA. jcarey@princeton.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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