ArticleJournal of molecular biology2010
P. aeruginosa PilT structures with and without nucleotide reveal a dynamic type IV pilus retraction motor.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 91 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
- Separation ofmBio · 2025Article
- Conformational changes in the motor ATPase CpaF facilitate a rotary mechanism of Tad pilus assembly.Nature communications · 2025Article
- Building permits-control of type IV pilus assembly by PilB and its cofactors.Journal of bacteriology · 2024Review
- 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
- A noncanonical cytochromeProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Carbon starvation of Pseudomonas aeruginosa biofilms selects for dispersal insensitive mutants.BMC microbiology · 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
- 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
- Electron Cryotomography of Bacterial Secretion Systems.Microbiology spectrum · 2019Article
- The Dynamic Structures of the Type IV Pilus.Microbiology spectrum · 2019Review
- Functional reconstitution of the type IVa pilus assembly system from enterohaemorrhagic Escherichia coli.Molecular microbiology · 2019Article
- X-ray crystal structures of the type IVb secretion system DotB ATPases.Protein science : a publication of the Protein Society · 2018Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Type IV pili are bacterial extracellular filaments that can be retracted to create force and motility. Retraction is accomplished by the motor protein PilT. Crystal structures of Pseudomonas aeruginosa PilT with and without bound beta,gamma-methyleneadenosine-5'-triphosphate have been solved at 2.6 A and 3.1 A resolution, respectively, revealing an interlocking hexamer formed by the action of a crystallographic 2-fold symmetry operator on three subunits in the asymmetric unit and held together by extensive ionic interactions. The roles of two invariant carboxylates, Asp Box motif Glu163 and Walker B motif Glu204, have been assigned to Mg(2+) binding and catalysis, respectively. The nucleotide ligands in each of the subunits in the asymmetric unit of the beta,gamma-methyleneadenosine-5'-triphosphate-bound PilT are not equally well ordered. Similarly, the three subunits in the asymmetric unit of both structures exhibit differing relative conformations of the two domains. The 12 degrees and 20 degrees domain rotations indicate motions that occur during the ATP-coupled mechanism of the disassembly of pili into membrane-localized pilin monomers. Integrating these observations, we propose a three-state "Ready, Active, Release" model for the action of PilT.
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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.