pubmed-article:15351654 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15351654 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
pubmed-article:15351654 | lifeskim:mentions | umls-concept:C0205177 | lld:lifeskim |
pubmed-article:15351654 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
pubmed-article:15351654 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
pubmed-article:15351654 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:15351654 | lifeskim:mentions | umls-concept:C0205173 | lld:lifeskim |
pubmed-article:15351654 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:15351654 | pubmed:dateCreated | 2004-9-7 | lld:pubmed |
pubmed-article:15351654 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15351654 | pubmed:abstractText | CheY is a member of the response regulator protein superfamily that controls the chemotactic swimming response of motile bacteria. The CheY double mutant D13K Y106W (CheY**) is resistant to phosphorylation, yet is a highly effective mimic of phosphorylated CheY in vivo and in vitro. The conformational attributes of this protein that enable it to signal in a phosphorylation-independent manner are unknown. We have solved the crystal structure of selenomethionine-substituted CheY** in the presence of its target, a peptide (FliM16) derived from the flagellar motor switch, FliM, to 1.5A resolution with an R-factor of 19.6%. The asymmetric unit contains four CheY** molecules, two with FliM16 bound, and two without. The two CheY** molecules in the asymmetric unit that are bound to FliM16 adopt a conformation similar to BeF3- -activated wild-type CheY, and also bind FliM16 in a nearly identical manner. The CheY** molecules that do not bind FliM16 are found in a conformation similar to unphosphorylated wild-type CheY, suggesting that the active phenotype of this mutant is enabled by a facile interconversion between the active and inactive conformations. Finally, we propose a ligand-binding model for CheY and CheY**, in which Ile95 changes conformation in a Tyr/Trp106-dependent manner to accommodate FliM. | lld:pubmed |
pubmed-article:15351654 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15351654 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15351654 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15351654 | pubmed:language | eng | lld:pubmed |
pubmed-article:15351654 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15351654 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:15351654 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15351654 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15351654 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15351654 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15351654 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15351654 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15351654 | pubmed:month | Sep | lld:pubmed |
pubmed-article:15351654 | pubmed:issn | 0022-2836 | lld:pubmed |
pubmed-article:15351654 | pubmed:author | pubmed-author:QuillinMichae... | lld:pubmed |
pubmed-article:15351654 | pubmed:author | pubmed-author:MatthewsBrian... | lld:pubmed |
pubmed-article:15351654 | pubmed:author | pubmed-author:DahlquistFred... | lld:pubmed |
pubmed-article:15351654 | pubmed:author | pubmed-author:HausrathAndre... | lld:pubmed |
pubmed-article:15351654 | pubmed:author | pubmed-author:MatsumuraPhil... | lld:pubmed |
pubmed-article:15351654 | pubmed:author | pubmed-author:LuJustineJ | lld:pubmed |
pubmed-article:15351654 | pubmed:author | pubmed-author:DyerCollin... | lld:pubmed |
pubmed-article:15351654 | pubmed:author | pubmed-author:CamposAndresA | lld:pubmed |
pubmed-article:15351654 | pubmed:author | pubmed-author:McEvoyMegan... | lld:pubmed |
pubmed-article:15351654 | pubmed:author | pubmed-author:WestbrookEdwi... | lld:pubmed |
pubmed-article:15351654 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15351654 | pubmed:day | 24 | lld:pubmed |
pubmed-article:15351654 | pubmed:volume | 342 | lld:pubmed |
pubmed-article:15351654 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15351654 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15351654 | pubmed:pagination | 1325-35 | lld:pubmed |
pubmed-article:15351654 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:15351654 | pubmed:meshHeading | pubmed-meshheading:15351654... | lld:pubmed |
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pubmed-article:15351654 | pubmed:meshHeading | pubmed-meshheading:15351654... | lld:pubmed |
pubmed-article:15351654 | pubmed:year | 2004 | lld:pubmed |
pubmed-article:15351654 | pubmed:articleTitle | Structure of the constitutively active double mutant CheYD13K Y106W alone and in complex with a FliM peptide. | lld:pubmed |
pubmed-article:15351654 | pubmed:affiliation | Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, USA. | lld:pubmed |
pubmed-article:15351654 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:15351654 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
entrez-gene:946393 | entrezgene:pubmed | pubmed-article:15351654 | lld:entrezgene |
entrez-gene:946442 | entrezgene:pubmed | pubmed-article:15351654 | lld:entrezgene |
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