Bacterial chemoreceptor arrays are hexagonally packed trimers of receptor dimers networked by rings of kinase and coupling proteins

Chemoreceptor arrays are supra molecular 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 arrange...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2012-03, Vol.109 (10), p.3766-3771
Main Authors: Briegel, Ariane, Li, Xiaoxiao, Bilwes, Alexandrine M., Hughes, Kelly T., Jensen, Grant J., Crane, Brian R.
Format: Article
Language:English
Subjects:
Bacillus subtilis - metabolism
Bacteria
Bacterial Physiological Phenomena
Bacterial Proteins - chemistry
Biological Sciences
Cells
CheA protein
Chemoreceptor Cells - cytology
Chemoreceptors
Chemotaxis
CheW protein
Crystal lattices
Crystal structure
Crystallization
Crystallography, X-Ray - methods
Crystals
Cytoplasm - metabolism
Dimerization
Dimers
Electron Microscope Tomography - methods
Escherichia coli
Escherichia coli - metabolism
Escherichia coli Proteins - chemistry
Histidine Kinase
Kinases
Membrane Proteins - chemistry
Membranes
Methyl-Accepting Chemotaxis Proteins
Protein Binding
Protein Conformation
Receptors
Salmonella enterica - metabolism
Signal transduction
T cell receptors
Trimers
X-ray crystallography
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Summary:Chemoreceptor arrays are supra molecular 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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1115719109