ArticleStructure (London, England : 1993)2014
Distinct docking and stabilization steps of the Pseudopilus conformational transition path suggest rotational assembly of type IV pilus-like fibers.
Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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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.
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Who cites it
27 citing papers in PubMed, 49 citations in OpenAlex.
- Detection of Protein-Protein Interactions in Escherichia coli With Single Molecule Sensitivity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Structural determinants of endopilus assembly, stability and functional specificity in bacterial type II secretion.bioRxiv : the preprint server for biology · 2026Article
- Membrane platform protein PulF of themBio · 2024Article
- Structure and Dynamics of Type 4a Pili and Type 2 Secretion System Endopili.Sub-cellular biochemistry · 2024Review
- PilY1 and minor pilins form a complex priming the type IVa pilus in Myxococcus xanthus.Nature communications · 2020Article
- Structure and Assembly of the Enterohemorrhagic Escherichia coli Type 4 Pilus.Structure (London, England : 1993) · 2019Article
- Dynamics of a type 2 secretion system pseudopilus unraveled by complementary approaches.Journal of biomolecular NMR · 2019Article
- Functional reconstitution of the type IVa pilus assembly system from enterohaemorrhagic Escherichia coli.Molecular microbiology · 2019Article
- Architecture, Function, and Substrates of the Type II Secretion System.EcoSal Plus · 2019Review
- Direct interactions between the secreted effector and the T2SS components GspL and GspM reveal a new effector-sensing step during type 2 secretion.The Journal of biological chemistry · 2018Article
- Structural cycle of the Thermus thermophilus PilF ATPase: the powering of type IVa pilus assembly.Scientific reports · 2018Article
- Structure of the calcium-dependent type 2 secretion pseudopilus.Nature microbiology · 2017Article
- Cryo-EM of bacterial pili and archaeal flagellar filaments.Current opinion in structural biology · 2017Review
- Predicting and Interpreting the Structure of Type IV Pilus of Electricigens by Molecular Dynamics Simulations.Molecules (Basel, Switzerland) · 2017Article
- Structure andeLife · 2017Article
- The molecular mechanism of the type IVa pilus motors.Nature communications · 2017Article
- Archaeal flagellin combines a bacterial type IV pilin domain with an Ig-like domain.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- A Comparative Structure/Function Analysis of Two Type IV Pilin DNA Receptors Defines a Novel Mode of DNA Binding.Structure (London, England : 1993) · 2016Article
- Low Energy Atomic Models Suggesting a Pilus Structure that could Account for Electrical Conductivity of Geobacter sulfurreducens Pili.Scientific reports · 2016Article
- Secretion systems in Gram-negative bacteria: structural and mechanistic insights.Nature reviews. Microbiology · 2015Review
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8 authors at 2 institutions in 2 countries.
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Abstract
The closely related bacterial type II secretion (T2S) and type IV pilus (T4P) systems are sophisticated machines that assemble dynamic fibers promoting protein transport, motility, or adhesion. Despite their essential role in virulence, the molecular mechanisms underlying helical fiber assembly remain unknown. Here, we use electron microscopy and flexible modeling to study conformational changes of PulG pili assembled by the Klebsiella oxytoca T2SS. Neural network analysis of 3,900 pilus models suggested a transition path toward low-energy conformations driven by progressive increase in fiber helical twist. Detailed predictions of interprotomer contacts along this path were tested by site-directed mutagenesis, pilus assembly, and protein secretion analyses. We demonstrate that electrostatic interactions between adjacent protomers (P-P+1) in the membrane drive pseudopilin docking, while P-P+3 and P-P+4 contacts determine downstream fiber stabilization steps. These results support a model of a spool-like assembly mechanism for fibers of the T2SS-T4P superfamily.
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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.