| pubmed-article:17720248 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17720248 | lifeskim:mentions | umls-concept:C0233820 | lld:lifeskim |
| pubmed-article:17720248 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:17720248 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:17720248 | lifeskim:mentions | umls-concept:C0037812 | lld:lifeskim |
| pubmed-article:17720248 | lifeskim:mentions | umls-concept:C0018966 | lld:lifeskim |
| pubmed-article:17720248 | lifeskim:mentions | umls-concept:C0018974 | lld:lifeskim |
| pubmed-article:17720248 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:17720248 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:17720248 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:17720248 | pubmed:issue | 11-12 | lld:pubmed |
| pubmed-article:17720248 | pubmed:dateCreated | 2007-10-22 | lld:pubmed |
| pubmed-article:17720248 | pubmed:abstractText | The bacterial CO-sensing heme protein CooA activates expression of genes whose products perform CO-metabolism by binding its target DNA in response to CO binding. The required conformational change has been proposed to result from CO-induced displacement of the heme and of the adjacent C-helix, which connects the sensory and DNA-binding domains. Support for this proposal comes from UV Resonance Raman (UVRR) spectroscopy, which reveals a more hydrophobic environment for the C-helix residue Trp110 when CO binds. In addition, we find a tyrosine UVRR response, which is attributable to weakening of a Tyr55-Glu83 H-bond that anchors the proximal side of the heme. Both Trp and Tyr responses are augmented in the heme domain when the DNA-binding domain has been removed, apparently reflecting loss of the inter-domain restraint. This augmentation is abolished by a Glu83Gln substitution, which weakens the anchoring H-bond. The CO recombination rate following photolysis of the CO adduct is similar for truncated and full-length protein, though truncation does increase the rate of CO association in the absence of photolysis; together these data indicate that truncation causes a faster dissociation of the endogenous Pro2 ligand. These findings are discussed in the light of structural evidence that the N-terminal tail, once released from the heme, selects the proper orientation of the DNA-binding domain, via docking interactions. | lld:pubmed |
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| pubmed-article:17720248 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17720248 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17720248 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17720248 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17720248 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17720248 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:17720248 | pubmed:issn | 0162-0134 | lld:pubmed |
| pubmed-article:17720248 | pubmed:author | pubmed-author:RobertsGary... | lld:pubmed |
| pubmed-article:17720248 | pubmed:author | pubmed-author:PoulosThomas... | lld:pubmed |
| pubmed-article:17720248 | pubmed:author | pubmed-author:SpiroThomas... | lld:pubmed |
| pubmed-article:17720248 | pubmed:author | pubmed-author:YounHwanH | lld:pubmed |
| pubmed-article:17720248 | pubmed:author | pubmed-author:KerbyRobert... | lld:pubmed |
| pubmed-article:17720248 | pubmed:author | pubmed-author:IbrahimMohamm... | lld:pubmed |
| pubmed-article:17720248 | pubmed:author | pubmed-author:KuchinskasMic... | lld:pubmed |
| pubmed-article:17720248 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17720248 | pubmed:volume | 101 | lld:pubmed |
| pubmed-article:17720248 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17720248 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17720248 | pubmed:pagination | 1776-85 | lld:pubmed |
| pubmed-article:17720248 | pubmed:dateRevised | 2011-9-26 | lld:pubmed |
| pubmed-article:17720248 | pubmed:meshHeading | pubmed-meshheading:17720248... | lld:pubmed |
| pubmed-article:17720248 | pubmed:meshHeading | pubmed-meshheading:17720248... | lld:pubmed |
| pubmed-article:17720248 | pubmed:meshHeading | pubmed-meshheading:17720248... | lld:pubmed |
| pubmed-article:17720248 | pubmed:meshHeading | pubmed-meshheading:17720248... | lld:pubmed |
| pubmed-article:17720248 | pubmed:meshHeading | pubmed-meshheading:17720248... | lld:pubmed |
| pubmed-article:17720248 | pubmed:meshHeading | pubmed-meshheading:17720248... | lld:pubmed |
| pubmed-article:17720248 | pubmed:meshHeading | pubmed-meshheading:17720248... | lld:pubmed |
| pubmed-article:17720248 | pubmed:meshHeading | pubmed-meshheading:17720248... | lld:pubmed |
| pubmed-article:17720248 | pubmed:meshHeading | pubmed-meshheading:17720248... | lld:pubmed |
| pubmed-article:17720248 | pubmed:meshHeading | pubmed-meshheading:17720248... | lld:pubmed |
| pubmed-article:17720248 | pubmed:meshHeading | pubmed-meshheading:17720248... | lld:pubmed |
| pubmed-article:17720248 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17720248 | pubmed:articleTitle | Mechanism of the CO-sensing heme protein CooA: new insights from the truncated heme domain and UVRR spectroscopy. | lld:pubmed |
| pubmed-article:17720248 | pubmed:affiliation | Department of Chemistry, Princeton University, Princeton, NJ 08544, USA. | lld:pubmed |
| pubmed-article:17720248 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17720248 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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