| pubmed-article:16929106 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16929106 | lifeskim:mentions | umls-concept:C0026377 | lld:lifeskim |
| pubmed-article:16929106 | pubmed:issue | Pt 9 | lld:pubmed |
| pubmed-article:16929106 | pubmed:dateCreated | 2006-8-24 | lld:pubmed |
| pubmed-article:16929106 | pubmed:abstractText | PhoB is an Escherichia coli transcription factor from a two-component signal transduction system that is sensitive to limiting environmental phosphate conditions. It consists of an N-terminal receiver domain (RD) and a C-terminal DNA-binding domain. The protein is activated upon phosphorylation at the RD, an event that depends on Mg(2+) binding. The structure of PhoB RD in complex with Mg(2+) is presented, which shows three protomers in the asymmetric unit that interact across two different surfaces. One association is symmetric and has been described as a non-active dimerization contact; the other involves the alpha4-beta5-alpha5 interface and recalls the contact found in activated PhoB. However, here this last interaction is not perfectly symmetric and helix alpha4, which in the activated molecule undergoes a helical shift, becomes strongly destabilized in one of the interacting monomers. All protomers bind the cation in a similar manner but, interestingly, at the prospective binding site for the phosphate moiety the side chains of either Glu88 (in helix alpha4) or Trp54 alternate and interact with active-site atoms. When Glu88 is inside the cavity, helix alpha4 is arranged similarly to the unliganded wild-type structure. However, if Trp54 is present, the helix loses its contacts with the active-site cavity and vanishes. Accordingly, the presence of Trp54 in the active site induces a flexible state in helix alpha4, potentially allowing a helical shift that phosphorylation would eventually stabilize. | lld:pubmed |
| pubmed-article:16929106 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16929106 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16929106 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16929106 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16929106 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16929106 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16929106 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:16929106 | pubmed:issn | 0907-4449 | lld:pubmed |
| pubmed-article:16929106 | pubmed:author | pubmed-author:CollMiquelM | lld:pubmed |
| pubmed-article:16929106 | pubmed:author | pubmed-author:Gomis-RüthF... | lld:pubmed |
| pubmed-article:16929106 | pubmed:author | pubmed-author:BlancoAlexand... | lld:pubmed |
| pubmed-article:16929106 | pubmed:author | pubmed-author:SolàMariaM | lld:pubmed |
| pubmed-article:16929106 | pubmed:author | pubmed-author:DrewDevin LDL | lld:pubmed |
| pubmed-article:16929106 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16929106 | pubmed:volume | 62 | lld:pubmed |
| pubmed-article:16929106 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16929106 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16929106 | pubmed:pagination | 1046-57 | lld:pubmed |
| pubmed-article:16929106 | pubmed:dateRevised | 2007-7-24 | lld:pubmed |
| pubmed-article:16929106 | pubmed:meshHeading | pubmed-meshheading:16929106... | lld:pubmed |
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| pubmed-article:16929106 | pubmed:meshHeading | pubmed-meshheading:16929106... | lld:pubmed |
| pubmed-article:16929106 | pubmed:meshHeading | pubmed-meshheading:16929106... | lld:pubmed |
| pubmed-article:16929106 | pubmed:meshHeading | pubmed-meshheading:16929106... | lld:pubmed |
| pubmed-article:16929106 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16929106 | pubmed:articleTitle | The cofactor-induced pre-active conformation in PhoB. | lld:pubmed |
| pubmed-article:16929106 | pubmed:affiliation | Institut de Biologia Molecular de Barcelona, CSIC, Parc Científic de Barcelona, c/ Josep Samitier 1-5, 08028 Barcelona, Spain. msvcri@ibmb.csic.es | lld:pubmed |
| pubmed-article:16929106 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16929106 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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