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 of the constitutively active double mutant CheYD13K Y106W alone and in complex with a FliM peptide.

Journal of molecular biology - 24 Sept 2004

Dyer Collin M, Quillin Michael L, Campos Andres, Lu Justine, McEvoy Megan M, Hausrath Andrew C, Westbrook Edwin M, Matsumura Philip, Matthews Brian W, Dahlquist Frederick W

Abstract excerpt

CheY is a member of the response regulator protein superfamily that controls the chemotactic swimming response of motile bacteria. The CheY double mutant D13K Y106W (CheY**) is resistant to phosphorylation, yet is a highly effective mimic of phosphorylated CheY in vivo and in vitro. The conformational attributes of this protein that enable it to signal in a phosphorylation-independent manner are unknown. We have...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Binding Sites

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

Share to Membrane Proteins

Share to Methyl-Accepting Chemotaxis Proteins

Share to Models, Molecular

Share to Phosphorylation

Share to Protein Conformation

Share to Tyrosine

Source

Identifiers

PMID: 15351654
DOI: 10.1016/j.jmb.2004.07.084

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 of the constitutively active double mutant CheYD13K Y106W alone and in complex with a FliM peptide.PMID 15351654Read ↗

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 ↗

Crystal structures of CheY mutants Y106W and T87I/Y106W. CheY activation correlates with movement of residue 106.Semantic proximity Read ↗

Correlated switch binding and signaling in bacterial chemotaxis.Semantic proximity Read ↗

A chemotactic signaling surface on CheY defined by suppressors of flagellar switch mutations.Semantic proximity Read ↗

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

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

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

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

Tyrosine 106 of CheY plays an important role in chemotaxis signal transduction in Escherichia coli.Semantic proximity Read ↗

The N terminus of FliM is essential to promote flagellar rotation in Rhodobacter sphaeroides.Semantic proximity Read ↗

Flagellar motor-switch binding face of CheY and the biochemical basis of suppression by CheY mutants that compensate for motor-switch defects in Escherichia coli.Semantic proximity Read ↗

Uncoupled phosphorylation and activation in bacterial chemotaxis. The 2.1-A structure of a threonine to isoleucine mutant at position 87 of CheY.Semantic proximity Read ↗

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