Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structure and catalytic mechanism of the E. coli chemotaxis phosphatase CheZ.

Nature structural biology - 1 Aug 2002

Zhao Rui, Collins Edward J, Bourret Robert B, Silversmith Ruth E

Abstract excerpt

The protein CheZ, which has the last unknown structure in the Escherichia coli chemotaxis pathway, stimulates the dephosphorylation of the response regulator CheY by an unknown mechanism. Here we report the co-crystal structure of CheZ with CheY, Mg(2+) and the phosphoryl analog, BeF(3)(-). The predominant structural feature of the CheZ dimer is a long four-helix bundle composed of two helices from each monomer....

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalysis
Share to Chemotaxis
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Macromolecular Substances

Share to Methyl-Accepting Chemotaxis Proteins

Share to Phosphoric Monoester Hydrolases

Share to ras Proteins

Share to Static Electricity

Source

Identifiers

PMID: 12080332
DOI: 10.1038/nsb816

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure and catalytic mechanism of the E. coli chemotaxis phosphatase CheZ.PMID 12080332Read ↗

Crystal structures of beryllium fluoride-free and beryllium fluoride-bound CheY in complex with the conserved C-terminal peptide of CheZ reveal dual binding modes specific to CheY conformation.Semantic proximity Read ↗

Phosphorylation-dependent binding of the chemotaxis signal molecule CheY to its phosphatase, CheZ.Semantic proximity Read ↗

Interaction of CheY with the C-terminal peptide of CheZ.Semantic proximity Read ↗

Structure and function of an unusual family of protein phosphatases: the bacterial chemotaxis proteins CheC and CheX.Semantic proximity Read ↗

Investigation of the role of electrostatic charge in activation of the Escherichia coli response regulator CheY.Semantic proximity Read ↗

Synthesis and biochemical characterization of a phosphorylated analogue of the response regulator CheB.Semantic proximity Read ↗

In vivo and in vitro characterization of Escherichia coli protein CheZ gain- and loss-of-function mutants.Semantic proximity Read ↗

Role of Position K+4 in the Phosphorylation and Dephosphorylation Reaction Kinetics of the CheY Response Regulator.Semantic proximity Read ↗

Roles of the highly conserved aspartate and lysine residues in the response regulator of bacterial chemotaxis.Semantic proximity Read ↗

Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis.Semantic proximity Read ↗

Conserved aspartate residues and phosphorylation in signal transduction by the chemotaxis protein CheY.Semantic proximity Read ↗

Isolation and characterization of nonchemotactic CheZ mutants of Escherichia coli.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.