Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2009-5-27
pubmed:databankReference
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.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-10466731, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-10481014, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-10676817, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-10798526, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-11295559, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-11983857, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-12064933, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-12186970, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-12453209, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-12595268, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-14967017, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-15187186, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-15539117, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-15573139, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-15683239, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-15802240, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-15909983, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-16171380, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-16267307, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-16622408, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-16879656, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-16959572, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-17144658, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-17217957, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-17299051, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-17360429, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-17994770, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-18165013, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-18363791, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-18621896, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-18689468, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-2254280, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-7910759, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-8563621, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-8831788, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-9585515, http://linkedlifedata.com/resource/pubmed/commentcorrection/19149470-9989504
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1520-4995
pubmed:author
pubmed:issnType
Electronic
pubmed:day
10
pubmed:volume
48
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1936-44
pubmed:dateRevised
2011-8-1
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
The structure of a soluble chemoreceptor suggests a mechanism for propagating conformational signals.
pubmed:affiliation
Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14850, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural