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

The Helix Rearrangement in the Periplasmic Domain of the Flagellar Stator B Subunit Activates Peptidoglycan Binding and Ion Influx.

Structure (London, England : 1993) - 3 Apr 2018

Kojima Seiji, Takao Masato, Almira Gaby, Kawahara Ikumi, Sakuma Mayuko, Homma Michio, Kojima Chojiro, Imada Katsumi

Abstract excerpt

The stator of the bacterial flagellar motor couples ion flow with torque generation. The ion-conducting stator channel opens only when incorporated into and anchored around the rotor via the peptidoglycan (PG) binding domain of the B subunit (MotBC). However, no direct evidence of PG binding coupled with channel activation has been presented. Here, we report the structural rearrangements of MotBC responsible for...

Read the complete abstract on PubMed

Topics

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

Share to Flagella
Share to Ion Transport

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Peptidoglycan

Share to Periplasm

Share to Protein Conformation, alpha-Helical

Share to Protein Conformation, beta-Strand

Share to Protons

Share to Salmonella enterica

Source

Identifiers

PMID: 29576320
DOI: 10.1016/j.str.2018.02.016

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Helix Rearrangement in the Periplasmic Domain of the Flagellar Stator B Subunit Activates Peptidoglycan Binding and Ion Influx.PMID 29576320Read ↗

Conformational change in the periplamic region of the flagellar stator coupled with the assembly around the rotor.Semantic proximity Read ↗

Structural analysis of variant of Helicobacter pylori MotB in its activated form, engineered as chimera of MotB and leucine zipper.Semantic proximity Read ↗

Flagellar movement driven by proton translocation.Semantic proximity Read ↗

Load-sensitive coupling of proton translocation and torque generation in the bacterial flagellar motor.Semantic proximity Read ↗

The role of a cytoplasmic loop of MotA in load-dependent assembly and disassembly dynamics of the MotA/B stator complex in the bacterial flagellar motor.Semantic proximity Read ↗

Mutations in the stator protein PomA affect switching of rotational direction in bacterial flagellar motor.Semantic proximity Read ↗

GFP Fusion to the N-Terminus of MotB Affects the Proton Channel Activity of the Bacterial Flagellar Motor in Salmonella.Semantic proximity Read ↗

<i>In situ</i> structures of periplasmic flagella in <i>Borrelia</i> reveals conformational changes essential for flagellar rotationSemantic proximity Read ↗

Dynamism and regulation of the stator, the energy conversion complex of the bacterial flagellar motor.Semantic proximity Read ↗

Structure of the MotA/B Proton Channel.Semantic proximity Read ↗

Conformational change in the stator of the bacterial flagellar motor.Semantic proximity Read ↗

Function of proline residues of MotA in torque generation by the flagellar motor of Escherichia coli.Semantic proximity Read ↗

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