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TitleBacterial chemoreceptor arrays are hexagonally packed trimers of receptor dimers networked by rings of kinase and coupling proteins.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 109, Issue 10, Page 3766-3771, Year 2012
Publish dateMar 6, 2012
AuthorsAriane Briegel / Xiaoxiao Li / Alexandrine M Bilwes / Kelly T Hughes / Grant J Jensen / Brian R Crane /
PubMed AbstractChemoreceptor arrays are supramolecular transmembrane machines of unknown structure that allow bacteria to sense their surroundings and respond by chemotaxis. We have combined X-ray crystallography ...Chemoreceptor arrays are supramolecular transmembrane machines of unknown structure that allow bacteria to sense their surroundings and respond by chemotaxis. We have combined X-ray crystallography of purified proteins with electron cryotomography of native arrays inside cells to reveal the arrangement of the component transmembrane receptors, histidine kinases (CheA) and CheW coupling proteins. Trimers of receptor dimers lie at the vertices of a hexagonal lattice in a "two-facing-two" configuration surrounding a ring of alternating CheA regulatory domains (P5) and CheW couplers. Whereas the CheA kinase domains (P4) project downward below the ring, the CheA dimerization domains (P3) link neighboring rings to form an extended, stable array. This highly interconnected protein architecture underlies the remarkable sensitivity and cooperative nature of transmembrane signaling in bacterial chemotaxis.
External linksProc Natl Acad Sci U S A / PubMed:22355139 / PubMed Central
MethodsEM (subtomogram averaging)
Structure data

EMDB-2158:
Bacterial chemoreceptor arrays are hexagonally packed trimers of receptor dimers networked by rings of kinase and coupling proteins
Method: EM (subtomogram averaging)

Source
  • Escherichia coli (E. coli)

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