ArticlePloS one2016
Molecular Models for the Core Components of the Flagellar Type-III Secretion Complex.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Structure of the cytoplasmic domain of SctV (SsaV) from the Salmonella SPI-2 injectisome and implications for a pH sensing mechanism.Journal of structural biology · 2021Article
- The substrate specificity switch FlhB assembles onto the export gate to regulate type three secretion.Nature communications · 2020Article
- High-resolution view of the type III secretion export apparatus in situ reveals membrane remodeling and a secretion pathway.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The Role of the Small Export Apparatus Protein, SctS, in the Activity of the Type III Secretion System.Frontiers in microbiology · 2019Article
- Structure of the core of the type III secretion system export apparatus.Nature structural & molecular biology · 2018Article
- Characterization of C-ring component assembly in flagellar motors from amino acid coevolution.Royal Society open science · 2018Article
- SimGen: A General Simulation Method for Large Systems.Journal of molecular biology · 2017Article
- Algorithms for matching partially labelled sequence graphs.Algorithms for molecular biology : AMB · 2017Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
We show that by using a combination of computational methods, consistent three-dimensional molecular models can be proposed for the core proteins of the type-III secretion system. We employed a variety of approaches to reconcile disparate, and sometimes inconsistent, data sources into a coherent picture that for most of the proteins indicated a unique solution to the constraints. The range of difficulty spanned from the trivial (FliQ) to the difficult (FlhA and FliP). The uncertainties encountered with FlhA were largely the result of the greater number of helix packing possibilities allowed in a large protein, however, for FliP, there remains an uncertainty in how to reconcile the large displacement predicted between its two main helical hairpins and their ability to sit together happily across the bacterial membrane. As there is still no high resolution structural information on any of these proteins, we hope our predicted models may be of some use in aiding the interpretation of electron microscope images and in rationalising mutation data and experiments.
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Registered trials
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