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Characterization of C-ring component assembly in flagellar motors from amino acid coevolution
Bacterial flagellar motility, an important virulence factor, is energized by a rotary motor localized within the flagellar basal body. The rotor module consists of a large framework (the C-ring), composed of the FliG, FliM and FliN proteins. FliN and FliM contacts the FliG torque ring to control the...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society Publishing
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5990795/ https://www.ncbi.nlm.nih.gov/pubmed/29892378 http://dx.doi.org/10.1098/rsos.171854 |
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author | dos Santos, Ricardo Nascimento Khan, Shahid Morcos, Faruck |
author_facet | dos Santos, Ricardo Nascimento Khan, Shahid Morcos, Faruck |
author_sort | dos Santos, Ricardo Nascimento |
collection | PubMed |
description | Bacterial flagellar motility, an important virulence factor, is energized by a rotary motor localized within the flagellar basal body. The rotor module consists of a large framework (the C-ring), composed of the FliG, FliM and FliN proteins. FliN and FliM contacts the FliG torque ring to control the direction of flagellar rotation. We report that structure-based models constrained only by residue coevolution can recover the binding interface of atomic X-ray dimer complexes with remarkable accuracy (approx. 1 Å RMSD). We propose a model for FliM–FliN heterodimerization, which agrees accurately with homologous interfaces as well as in situ cross-linking experiments, and hence supports a proposed architecture for the lower portion of the C-ring. Furthermore, this approach allowed the identification of two discrete and interchangeable homodimerization interfaces between FliM middle domains that agree with experimental measurements and might be associated with C-ring directional switching dynamics triggered upon binding of CheY signal protein. Our findings provide structural details of complex formation at the C-ring that have been difficult to obtain with previous methodologies and clarify the architectural principle that underpins the ultra-sensitive allostery exhibited by this ring assembly that controls the clockwise or counterclockwise rotation of flagella. |
format | Online Article Text |
id | pubmed-5990795 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | The Royal Society Publishing |
record_format | MEDLINE/PubMed |
spelling | pubmed-59907952018-06-11 Characterization of C-ring component assembly in flagellar motors from amino acid coevolution dos Santos, Ricardo Nascimento Khan, Shahid Morcos, Faruck R Soc Open Sci Biochemistry and Biophysics Bacterial flagellar motility, an important virulence factor, is energized by a rotary motor localized within the flagellar basal body. The rotor module consists of a large framework (the C-ring), composed of the FliG, FliM and FliN proteins. FliN and FliM contacts the FliG torque ring to control the direction of flagellar rotation. We report that structure-based models constrained only by residue coevolution can recover the binding interface of atomic X-ray dimer complexes with remarkable accuracy (approx. 1 Å RMSD). We propose a model for FliM–FliN heterodimerization, which agrees accurately with homologous interfaces as well as in situ cross-linking experiments, and hence supports a proposed architecture for the lower portion of the C-ring. Furthermore, this approach allowed the identification of two discrete and interchangeable homodimerization interfaces between FliM middle domains that agree with experimental measurements and might be associated with C-ring directional switching dynamics triggered upon binding of CheY signal protein. Our findings provide structural details of complex formation at the C-ring that have been difficult to obtain with previous methodologies and clarify the architectural principle that underpins the ultra-sensitive allostery exhibited by this ring assembly that controls the clockwise or counterclockwise rotation of flagella. The Royal Society Publishing 2018-05-09 /pmc/articles/PMC5990795/ /pubmed/29892378 http://dx.doi.org/10.1098/rsos.171854 Text en © 2018 The Authors. http://creativecommons.org/licenses/by/4.0/ Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited. |
spellingShingle | Biochemistry and Biophysics dos Santos, Ricardo Nascimento Khan, Shahid Morcos, Faruck Characterization of C-ring component assembly in flagellar motors from amino acid coevolution |
title | Characterization of C-ring component assembly in flagellar motors from amino acid coevolution |
title_full | Characterization of C-ring component assembly in flagellar motors from amino acid coevolution |
title_fullStr | Characterization of C-ring component assembly in flagellar motors from amino acid coevolution |
title_full_unstemmed | Characterization of C-ring component assembly in flagellar motors from amino acid coevolution |
title_short | Characterization of C-ring component assembly in flagellar motors from amino acid coevolution |
title_sort | characterization of c-ring component assembly in flagellar motors from amino acid coevolution |
topic | Biochemistry and Biophysics |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5990795/ https://www.ncbi.nlm.nih.gov/pubmed/29892378 http://dx.doi.org/10.1098/rsos.171854 |
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