Molecular Models for the Core Components of the Flagellar Type-III Secretion Complex
| Autor: | Morgan Beeby, Teige R. S. Matthews-Palmer, William R. Taylor |
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| Přispěvatelé: | The Royal Society, Commission of the European Communities |
| Rok vydání: | 2016 |
| Předmět: |
Models
Molecular 0301 basic medicine Molecular model lcsh:Medicine Secretion Systems Protein Structure Prediction Web Browser Pathology and Laboratory Medicine Biochemistry Mathematical and Statistical Techniques Microbial Physiology Databases Genetic Type III Secretion Systems Macromolecular Structure Analysis Medicine and Health Sciences Bacterial Physiology lcsh:Science Physics Multidisciplinary Core component Flagella Physical Sciences Mutation (genetic algorithm) Pathogens Biological system Sequence Analysis Statistics (Mathematics) Research Article Multiple Alignment Calculation Protein Structure General Science & Technology Virulence Factors Type (model theory) Research and Analysis Methods Models Biological Microbiology Evolution Molecular Structure-Activity Relationship 03 medical and health sciences Bacterial Proteins MD Multidisciplinary Computational Techniques Secretion Statistical Methods Molecular Biology Techniques Sequencing Techniques Molecular Biology lcsh:R Computational Biology Biology and Life Sciences Proteins Bacteriology Core protein Split-Decomposition Method Range (mathematics) 030104 developmental biology Multiprotein Complexes Helix lcsh:Q Globular Proteins Sequence Alignment Mathematics Forecasting |
| Zdroj: | PLoS ONE, Vol 11, Iss 11, p e0164047 (2016) PLoS ONE |
| ISSN: | 1932-6203 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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