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

A slight bending of an α-helix in FliM creates a counterclockwise-locked structure of the flagellar motor in Vibrio.

Journal of biochemistry - 4 Dec 2021

Takekawa Norihiro, Nishikino Tatsuro, Yamashita Toshiki, Hori Kiyoshiro, Onoue Yasuhiro, Ihara Kunio, Kojima Seiji, Homma Michio, Imada Katsumi

Abstract excerpt

Many bacteria swim by rotating flagella. The chemotaxis system controls the direction of flagellar rotation. Vibrio alginolyticus, which has a single polar flagellum, swims smoothly by rotating the flagellar motor counterclockwise (CCW) in response to attractants. In response to repellents, the motor frequently switches its rotational direction between CCW and clockwise (CW). We isolated a mutant strain that...

Topics

Bacterial Proteins
Chemotaxis
Crystallography, X-Ray
Flagella
Models, Molecular
Molecular Motor Proteins
Mutation
Phosphorylation
Protein Binding
Protein Conformation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Conformation, alpha-Helical

Rotation

Vibrio alginolyticus

Whole Genome Sequencing

Source

Identifiers

PMID: 34143212
DOI: 10.1093/jb/mvab074

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A slight bending of an α-helix in FliM creates a counterclockwise-locked structure of the flagellar motor in Vibrio.PMID 34143212Read ↗

Structural insight into the rotational switching mechanism of the bacterial flagellar motor.Semantic proximity Read ↗

Effect of FliG three amino acids deletion in Vibrio polar-flagellar rotation and formation.Semantic proximity Read ↗

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

Molecular Mechanism for Rotational Switching of the Bacterial Flagellar MotorSemantic proximity Read ↗

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

Regulatory Role of a Hydrophobic Core in the FliG C-Terminal Domain in the Rotary Direction of a Flagellar Motor.Semantic proximity Read ↗

ZomB is essential for flagellar motor reversals in Shewanella putrefaciens and Vibrio parahaemolyticus.Semantic proximity Read ↗

The Gearbox of the Bacterial Flagellar Motor Switch.Semantic proximity Read ↗

Subunit organization and reversal-associated movements in the flagellar switch of Escherichia coli.Semantic proximity Read ↗

Mutational analysis of the flagellar rotor protein FliN: identification of surfaces important for flagellar assembly and switching.Semantic proximity Read ↗

Formation of multiple flagella caused by a mutation of the flagellar rotor protein FliM in Vibrio alginolyticus.Semantic proximity Read ↗

An extreme clockwise switch bias mutation in fliG of Salmonella typhimurium and its suppression by slow-motile mutations in motA and motB.Semantic proximity Read ↗

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