ArticleStructure (London, England : 1993)2007
Crystal structures of the pilus retraction motor PilT suggest large domain movements and subunit cooperation drive motility.
Article in Structure (London, England : 1993), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
77 citing papers in PubMed, 138 citations in OpenAlex.
- 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
- Analysis of the heterogenous structural states of the hexameric ATPase PilU of the Type IV pili frombioRxiv : the preprint server for biology · 2026Article
- Article
- Conformational changes in the motor ATPase CpaF facilitate a rotary mechanism of Tad pilus assembly.Nature communications · 2025Article
- The role of PilU in the surface behaviors ofmLife · 2025Article
- Combinatorial control of type IVa pili formation by the four polarized regulators MglA, SgmX, FrzS, and SopA.Journal of bacteriology · 2024Article
- Bidirectional pilus processing in the Tad pilus system motor CpaF.Nature communications · 2024Article
- A bacterial sense of touch: T4P retraction motor as a means of surface sensing byJournal of bacteriology · 2024Review
- Genome analysis and hyphal movement characterization of the hitchhiker endohyphalApplied and environmental microbiology · 2024Article
- Type IV pilus retraction is required formBio · 2024Article
- The genome sequence of Synechocystis sp. PCC 6803 substrain GT-T and its implications for the evolution of PCC 6803 substrains.FEBS open bio · 2023Article
- Landmark Discoveries and Recent Advances in Type IV Pilus Research.Microbiology and molecular biology reviews : MMBR · 2022Review
- The PilB-PilZ-FimX regulatory complex of the Type IV pilus from Xanthomonas citri.PLoS pathogens · 2021Article
- The small GTPase MglA together with the TPR domain protein SgmX stimulates type IV pili formation inProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Core architecture of a bacterial type II secretion system.Nature communications · 2019Article
- Multiple conformations facilitate PilT function in the type IV pilus.Nature communications · 2019Article
- PilT and PilU are homohexameric ATPases that coordinate to retract type IVa pili.PLoS genetics · 2019Article
- Motor Properties of PilT-Independent Type 4 Pilus Retraction in Gonococci.Journal of bacteriology · 2019Article
- The type IV pilus protein PilU functions as a PilT-dependent retraction ATPase.PLoS genetics · 2019Article
- Type IV pili: dynamics, biophysics and functional consequences.Nature reviews. Microbiology · 2019Review
17 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
PilT is a hexameric ATPase required for bacterial type IV pilus retraction and surface motility. Crystal structures of ADP- and ATP-bound Aquifex aeolicus PilT at 2.8 and 3.2 A resolution show N-terminal PAS-like and C-terminal RecA-like ATPase domains followed by a set of short C-terminal helices. The hexamer is formed by extensive polar subunit interactions between the ATPase core of one monomer and the N-terminal domain of the next. An additional structure captures a nonsymmetric PilT hexamer in which approach of invariant arginines from two subunits to the bound nucleotide forms an enzymatically competent active site. A panel of pilT mutations highlights the importance of the arginines, the PAS-like domain, the polar subunit interface, and the C-terminal helices for retraction. We present a model for ATP binding leading to dramatic PilT domain motions, engagement of the arginine wire, and subunit communication in this hexameric motor. Our conclusions apply to the entire type II/IV secretion ATPase family.
Indexed as
Identifiers
What OpenQuestion holds
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.