| pubmed-article:11013219 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11013219 | lifeskim:mentions | umls-concept:C0009235 | lld:lifeskim |
| pubmed-article:11013219 | lifeskim:mentions | umls-concept:C0040648 | lld:lifeskim |
| pubmed-article:11013219 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:11013219 | lifeskim:mentions | umls-concept:C0332462 | lld:lifeskim |
| pubmed-article:11013219 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:11013219 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:11013219 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:11013219 | pubmed:dateCreated | 2000-12-8 | lld:pubmed |
| pubmed-article:11013219 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11013219 | pubmed:abstractText | FadR is a dimeric acyl coenzyme A (acyl CoA)-binding protein and transcription factor that regulates the expression of genes encoding fatty acid biosynthetic and degrading enzymes in Escherichia coli. Here, the 2.0 A crystal structure of full-length FadR is described, determined using multi-wavelength anomalous dispersion. The structure reveals a dimer and a two-domain fold, with DNA-binding and acyl-CoA-binding sites located in an N-terminal and C-terminal domain, respectively. The N-terminal domain contains a winged helix-turn-helix prokaryotic DNA-binding fold. Comparison with known structures and analysis of mutagenesis data delineated the site of interaction with DNA. The C-terminal domain has a novel fold, consisting of a seven-helical bundle with a crossover topology. Careful analysis of the structure, together with mutational and biophysical data, revealed a putative hydrophobic acyl-CoA-binding site, buried in the core of the seven-helical bundle. This structure aids in understanding FadR function at a molecular level, provides the first structural scaffold for the large GntR family of transcription factors, which are keys in the control of metabolism in bacterial pathogens, and could thus be a possible target for novel chemotherapeutic agents. | lld:pubmed |
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| pubmed-article:11013219 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11013219 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11013219 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11013219 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11013219 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11013219 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11013219 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11013219 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11013219 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11013219 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11013219 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11013219 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:11013219 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:11013219 | pubmed:author | pubmed-author:KnudsenJJ | lld:pubmed |
| pubmed-article:11013219 | pubmed:author | pubmed-author:WierengaR KRK | lld:pubmed |
| pubmed-article:11013219 | pubmed:author | pubmed-author:DiRussoC CCC | lld:pubmed |
| pubmed-article:11013219 | pubmed:author | pubmed-author:van AaltenD... | lld:pubmed |
| pubmed-article:11013219 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11013219 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:11013219 | pubmed:volume | 19 | lld:pubmed |
| pubmed-article:11013219 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11013219 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11013219 | pubmed:pagination | 5167-77 | lld:pubmed |
| pubmed-article:11013219 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:11013219 | pubmed:meshHeading | pubmed-meshheading:11013219... | lld:pubmed |
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| pubmed-article:11013219 | pubmed:meshHeading | pubmed-meshheading:11013219... | lld:pubmed |
| pubmed-article:11013219 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11013219 | pubmed:articleTitle | Crystal structure of FadR, a fatty acid-responsive transcription factor with a novel acyl coenzyme A-binding fold. | lld:pubmed |
| pubmed-article:11013219 | pubmed:affiliation | Wellcome Trust Biocentre, Department of Biochemistry, University of Dundee, Dow Street, Dundee DD1 5EH, UK. dava@davapc1.bioch.dundee.ac.uk | lld:pubmed |
| pubmed-article:11013219 | pubmed:publicationType | Journal Article | lld:pubmed |
