ArticleNature communications2017
The molecular mechanism of the type IVa pilus motors.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.
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Who cites it
85 citing papers in PubMed, 145 citations in OpenAlex.
- A broad-spectrum phage-encoded mechanism to disarm bacterial type IV filaments.PLoS pathogens · 2026Article
- Structural modeling reveals the mechanism of motor ATPase coordination during type IV pilus retraction.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Analysis of the heterogenous structural states of the hexameric ATPase PilU of the type IV pili from Vibrio cholerae.Protein science : a publication of the Protein Society · 2026Article
- Article
- Structural insights into the Thermus thermophilus type IV pilus machinery assembling two distinct pili.Communications biology · 2026Article
- A broad-spectrum phage-encoded mechanism to disarm bacterial type IV filaments.bioRxiv : the preprint server for biology · 2026Article
- Analysis of the heterogenous structural states of the hexameric ATPase PilU of the Type IV pili frombioRxiv : the preprint server for biology · 2026Article
- CRISPR-Cas-Mediated Reprogramming Strategies to Overcome Antimicrobial Resistance.Pharmaceutics · 2026Review
- Characterization and Genomic Analysis ofAnimals : an open access journal from MDPI · 2025Article
- Separation ofmBio · 2025Article
- Integrative Structure and Function of thebioRxiv : the preprint server for biology · 2025Article
- Twitching motility suppressors reveal a role for FimX in type IV pilus extension dynamics.PLoS genetics · 2025Article
- Milestones in the development ofJournal of bacteriology · 2025Review
- Beyond movement: the dynamic roles of Type IV pili in cyanobacterial life.Journal of bacteriology · 2025Review
- Nitrosarchaeum haohaiensis sp. Nov. CL1Environmental microbiology reports · 2025Article
- Conformational changes in the motor ATPase CpaF facilitate a rotary mechanism of Tad pilus assembly.Nature communications · 2025Article
- The molecular basis for DNA-binding by competence T4P is distinct in a representative Gram-positive and Gram-negative species.PLoS pathogens · 2025Article
- Hyperpiliation, not loss of pilus retraction, reducesMicrobiology spectrum · 2025Article
- How Does the Archaellum Work?Biomolecules · 2025Review
- The role of PilU in the surface behaviors ofmLife · 2025Article
25 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type IVa pili are protein filaments essential for virulence in many bacterial pathogens; they extend and retract from the surface of bacterial cells to pull the bacteria forward. The motor ATPase PilB powers pilus assembly. Here we report the structures of the core ATPase domains of Geobacter metallireducens PilB bound to ADP and the non-hydrolysable ATP analogue, AMP-PNP, at 3.4 and 2.3 Å resolution, respectively. These structures reveal important differences in nucleotide binding between chains. Analysis of these differences reveals the sequential turnover of nucleotide, and the corresponding domain movements. Our data suggest a clockwise rotation of the central sub-pores of PilB, which through interactions with PilC, would support the assembly of a right-handed helical pilus. Our analysis also suggests a counterclockwise rotation of the C2 symmetric PilT that would enable right-handed pilus disassembly. The proposed model provides insight into how this family of ATPases can power pilus extension and retraction.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.