Source:http://linkedlifedata.com/resource/pubmed/id/11279025
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
20
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pubmed:dateCreated |
2001-5-23
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pubmed:databankReference | |
pubmed:abstractText |
In Escherichia coli, the expression of fatty acid metabolic genes is controlled by the transcription factor, FadR. The affinity of FadR for DNA is controlled by long chain acyl-CoA molecules, which bind to the protein and modulate gene expression. The crystal structure of FadR reveals a two domain dimeric molecule where the N-terminal domains bind DNA, and the C-terminal domains bind acyl-CoA. The DNA binding domain has a winged-helix motif, and the C-terminal domain resembles the sensor domain of the Tet repressor. The FadR.DNA complex reveals how the protein interacts with DNA and specifically recognizes a palindromic sequence. Structural and functional similarities to the Tet repressor and the BmrR transcription factors suggest how the binding of the acyl-CoA effector molecule to the C-terminal domain may affect the DNA binding affinity of the N-terminal domain. We suggest that the binding of acyl-CoA disrupts a buried network of charged and polar residues in the C-terminal domain, and the resulting conformational change is transmitted to the N-terminal domain via a domain-spanning alpha-helix.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acyl Coenzyme A,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/FadR protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
17373-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11279025-Acyl Coenzyme A,
pubmed-meshheading:11279025-Bacterial Proteins,
pubmed-meshheading:11279025-Binding Sites,
pubmed-meshheading:11279025-Crystallography, X-Ray,
pubmed-meshheading:11279025-DNA, Bacterial,
pubmed-meshheading:11279025-Escherichia coli,
pubmed-meshheading:11279025-Gene Expression Regulation, Bacterial,
pubmed-meshheading:11279025-Models, Molecular,
pubmed-meshheading:11279025-Nucleic Acid Conformation,
pubmed-meshheading:11279025-Protein Structure, Secondary,
pubmed-meshheading:11279025-Recombinant Proteins,
pubmed-meshheading:11279025-Repressor Proteins,
pubmed-meshheading:11279025-Transcription Factors
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pubmed:year |
2001
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pubmed:articleTitle |
The FadR.DNA complex. Transcriptional control of fatty acid metabolism in Escherichia coli.
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pubmed:affiliation |
Department of Structural Biology, St Jude Children's Research Hospital, Memphis, Tennessee 38105, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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