Structure of CheA, a signal-transducing histidine kinase (Q27766893)

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L A Alex

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B R Crane

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M I Simon

Protein histidine kinases and signal transduction in prokaryotes and eukaryotes

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language of work or name

English

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publication date

8 January 1999

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published in

Cell

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volume

96

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issue

1

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page(s)

131-41

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cites work

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DNA topology: topoisomerases keep it simple

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The carboxy-terminal portion of the CheA kinase mediates regulation of autophosphorylation by transducer and CheW.

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Initiation of sporulation in B. subtilis is controlled by a multicomponent phosphorelay

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Dual chemotaxis signaling pathways in Bacillus subtilis: a sigma D-dependent gene encodes a novel protein with both CheW and CheY homologous domains

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Signal transduction in bacteria: CheW forms a reversible complex with the protein kinase CheA

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Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis

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The Entropic Penalty of Ordered Water Accounts for Weaker Binding of the Antibiotic Novobiocin to a Resistant Mutant of DNA Gyrase: A Thermodynamic and Crystallographic Study

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Mutants defective in bacterial chemotaxis show modified protein phosphorylation

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Intermolecular complementation of the kinase activity of CheA.

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Expression of CheA fragments which define domains encoding kinase, phosphotransfer, and CheY binding activities

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Formation of a novel four-helix bundle and molecular recognition sites by dimerization of a response regulator phosphotransferase

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Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY

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Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR.

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NMR studies of the phosphotransfer domain of the histidine kinase CheA from Escherichia coli: assignments, secondary structure, general fold, and backbone dynamics

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

9989504

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Consolidated OpenCitations Corpus – April 2017