| pubmed-article:19149470 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19149470 | lifeskim:mentions | umls-concept:C0008010 | lld:lifeskim |
| pubmed-article:19149470 | lifeskim:mentions | umls-concept:C1749467 | lld:lifeskim |
| pubmed-article:19149470 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:19149470 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:19149470 | lifeskim:mentions | umls-concept:C1705535 | lld:lifeskim |
| pubmed-article:19149470 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:19149470 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:19149470 | pubmed:dateCreated | 2009-5-27 | lld:pubmed |
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| pubmed-article:19149470 | pubmed:abstractText | Transmembrane chemoreceptors, also known as methyl-accepting chemotaxis proteins (MCPs), translate extracellular signals into intracellular responses in the bacterial chemotaxis system. MCP ligand binding domains control the activity of the CheA kinase, situated approximately 200 A away, across the cytoplasmic membrane. The 2.17 A resolution crystal structure of a Thermotoga maritima soluble receptor (Tm14) reveals distortions in its dimeric four-helix bundle that provide insight into the conformational states available to MCPs for propagating signals. A bulge in one helix generates asymmetry between subunits that displaces the kinase-interacting tip, which resides more than 100 A away. The maximum bundle distortion maps to the adaptation region of transmembrane MCPs where reversible methylation of acidic residues tunes receptor activity. Minor alterations in coiled-coil packing geometry translate the bulge distortion to a >25 A movement of the tip relative to the bundle stalks. The Tm14 structure discloses how alterations in local helical structure, which could be induced by changes in methylation state and/or by conformational signals from membrane proximal regions, can reposition a remote domain that interacts with the CheA kinase. | lld:pubmed |
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| pubmed-article:19149470 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:19149470 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19149470 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19149470 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:19149470 | pubmed:issn | 1520-4995 | lld:pubmed |
| pubmed-article:19149470 | pubmed:author | pubmed-author:BilwesAlexand... | lld:pubmed |
| pubmed-article:19149470 | pubmed:author | pubmed-author:CraneBrian... | lld:pubmed |
| pubmed-article:19149470 | pubmed:author | pubmed-author:PollardAbiola... | lld:pubmed |
| pubmed-article:19149470 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19149470 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:19149470 | pubmed:volume | 48 | lld:pubmed |
| pubmed-article:19149470 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19149470 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19149470 | pubmed:pagination | 1936-44 | lld:pubmed |
| pubmed-article:19149470 | pubmed:dateRevised | 2011-8-1 | lld:pubmed |
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| pubmed-article:19149470 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19149470 | pubmed:articleTitle | The structure of a soluble chemoreceptor suggests a mechanism for propagating conformational signals. | lld:pubmed |
| pubmed-article:19149470 | pubmed:affiliation | Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14850, USA. | lld:pubmed |
| pubmed-article:19149470 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19149470 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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