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

Molecular Basis of the Interaction between the Flagellar Export Proteins FliI and FliH from Helicobacter pylori

31 Oct 2005

Abstract excerpt

Bacterial flagellar protein export requires an ATPase, FliI, and presumptive inhibitor, FliH. We have explored the molecular basis for FliI/FliH interaction in the human gastric pathogen Helicobacter pylori. By using bioinformatic and biochemical analyses, we showed that residues 1-18 of FliI very likely form an amphipathic alpha-helix upon interaction with FliH, and that residues 21-91 of FliI resemble the...

Read the complete abstract on PubMed

Topics

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

Share to Enzyme Structure and Function
Share to Helicobacter pylori-related gastroenterology studies
Share to Microbial Metabolites in Food Biotechnology

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

Source

Identifiers

PMID: 16260786
DOI: 10.1074/jbc.m507238200

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

Molecular Basis of the Interaction between the Flagellar Export Proteins FliI and FliH from Helicobacter pyloriPMID 16260786Read ↗

Requirement of the flagellar protein export apparatus component FliO for optimal expression of flagellar genes in Helicobacter pylori.Semantic proximity Read ↗

A flagellar-specific ATPase (FliI) is necessary for flagellar export in Helicobacter pylori.Semantic proximity Read ↗

Interaction between FliJ and FlhA, components of the bacterial flagellar type III export apparatus.Semantic proximity Read ↗

Genetic characterization of conserved charged residues in the bacterial flagellar type III export protein FlhA.Semantic proximity Read ↗

Intrinsic membrane targeting of the flagellar export ATPase FliI: interaction with acidic phospholipids and FliH.Semantic proximity Read ↗

Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export.Semantic proximity Read ↗

The FliN-FliH interaction mediates localization of flagellar export ATPase FliI to the C ring complex.Semantic proximity Read ↗

Weak Interactions between Salmonella enterica FlhB and Other Flagellar Export Apparatus Proteins Govern Type III Secretion Dynamics.Semantic proximity Read ↗

FliH, a soluble component of the type III flagellar export apparatus of Salmonella, forms a complex with FliI and inhibits its ATPase activity.Semantic proximity Read ↗

Interactions of FliJ with the Salmonella type III flagellar export apparatus.Semantic proximity Read ↗

Assembly dynamics and the roles of FliI ATPase of the bacterial flagellar export apparatus.Semantic proximity Read ↗

Cloning and characterization of the Helicobacter pylori flbA gene, which codes for a membrane protein involved in coordinated expression of flagellar genes.Semantic proximity Read ↗

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