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 structure of the periplasmic FlaG-FlaF complex and its essential role for archaellar swimming motility.

Nature microbiology - 1 Jan 2020

Tsai Chi-Lin, Tripp Patrick, Sivabalasarma Shamphavi, Zhang Changyi, Rodriguez-Franco Marta, Wipfler Rebecca L, Chaudhury Paushali, Banerjee Ankan, Beeby Morgan, Whitaker Rachel J, Tainer John A, Albers Sonja-Verena

Abstract excerpt

Motility structures are vital in all three domains of life. In Archaea, motility is mediated by the archaellum, a rotating type IV pilus-like structure that is a unique nanomachine for swimming motility in nature. Whereas periplasmic FlaF binds the surface layer (S-layer), the structure, assembly and roles of other periplasmic components remain enigmatic, limiting our knowledge of the archaellum's functional...

Read the complete abstract on PubMed

Topics

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

Share to Archaeal Proteins
Share to Flagella

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Movement

Share to Periplasm

Share to Protein Folding

Share to Protein Interaction Domains and Motifs

Share to Protein Multimerization

Share to Protein Processing, Post-Translational

Source

Open in PubMed Open full text

Identifiers

PMID: 31844299
DOI: 10.1038/s41564-019-0622-3
PMCID: PMC6952060

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The structure of the periplasmic FlaG-FlaF complex and its essential role for archaellar swimming motility.PMID 31844299Read ↗

FlaF Is a β-Sandwich Protein that Anchors the Archaellum in the Archaeal Cell Envelope by Binding the S-Layer Protein.Semantic proximity Read ↗

Flagellar motility and structure in the hyperthermoacidophilic archaeon Sulfolobus solfataricus.Semantic proximity Read ↗

Characterization of the flagellar collar reveals structural plasticity essential for spirochete motilitySemantic proximity Read ↗

Structure and function of the adhesive type IV pilus of Sulfolobus acidocaldarius.Semantic proximity Read ↗

FlcE latches onto the FliL-stator complex to turbocharge flagellar motility in <i>Borrelia burgdorferi</i>Semantic proximity Read ↗

Two residues predominantly dictate functional difference in motility between Shewanella oneidensis flagellins FlaA and FlaB.Semantic proximity Read ↗

A structural model of flagellar filament switching across multiple bacterial species.Semantic proximity Read ↗

The structure of the Vibrio alginolyticus flagellar filament suggests molecular mechanism for the rotation of sheathed flagellaSemantic proximity Read ↗

PilY1 and minor pilins form a complex priming the type IVa pilus in Myxococcus xanthus.Semantic proximity Read ↗

Structural insights into the biogenesis and biofilm formation by the Escherichia coli common pilus.Semantic proximity Read ↗

Structural basis for curvature generation and functional specialization in spirochete flagellaSemantic proximity Read ↗

Molecular and structural innovations of the stator motor complex at the dawn of flagellar motilitySemantic proximity Read ↗

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