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Structure and Assembly of the Proteus mirabilis Flagellar Motor by Cryo-Electron Tomography

Proteus mirabilis is a Gram-negative Gammaproteobacterium and a major causative agent of urinary tract infections in humans. It is characterized by its ability to switch between swimming motility in liquid media and swarming on solid surfaces. Here, we used cryo-electron tomography and subtomogram a...

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Autores principales: Kaplan, Mohammed, Yao, Qing, Jensen, Grant J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10179241/
https://www.ncbi.nlm.nih.gov/pubmed/37176000
http://dx.doi.org/10.3390/ijms24098292
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author Kaplan, Mohammed
Yao, Qing
Jensen, Grant J.
author_facet Kaplan, Mohammed
Yao, Qing
Jensen, Grant J.
author_sort Kaplan, Mohammed
collection PubMed
description Proteus mirabilis is a Gram-negative Gammaproteobacterium and a major causative agent of urinary tract infections in humans. It is characterized by its ability to switch between swimming motility in liquid media and swarming on solid surfaces. Here, we used cryo-electron tomography and subtomogram averaging to reveal the structure of the flagellar motor of P. mirabilis at nanometer resolution in intact cells. We found that P. mirabilis has a motor that is structurally similar to those of Escherichia coli and Salmonella enterica, lacking the periplasmic elaborations that characterize other more specialized gammaproteobacterial motors. In addition, no density corresponding to stators was present in the subtomogram average suggesting that the stators are dynamic. Finally, several assembly intermediates of the motor were seen that support the inside-out assembly pathway.
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spelling pubmed-101792412023-05-13 Structure and Assembly of the Proteus mirabilis Flagellar Motor by Cryo-Electron Tomography Kaplan, Mohammed Yao, Qing Jensen, Grant J. Int J Mol Sci Brief Report Proteus mirabilis is a Gram-negative Gammaproteobacterium and a major causative agent of urinary tract infections in humans. It is characterized by its ability to switch between swimming motility in liquid media and swarming on solid surfaces. Here, we used cryo-electron tomography and subtomogram averaging to reveal the structure of the flagellar motor of P. mirabilis at nanometer resolution in intact cells. We found that P. mirabilis has a motor that is structurally similar to those of Escherichia coli and Salmonella enterica, lacking the periplasmic elaborations that characterize other more specialized gammaproteobacterial motors. In addition, no density corresponding to stators was present in the subtomogram average suggesting that the stators are dynamic. Finally, several assembly intermediates of the motor were seen that support the inside-out assembly pathway. MDPI 2023-05-05 /pmc/articles/PMC10179241/ /pubmed/37176000 http://dx.doi.org/10.3390/ijms24098292 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Brief Report
Kaplan, Mohammed
Yao, Qing
Jensen, Grant J.
Structure and Assembly of the Proteus mirabilis Flagellar Motor by Cryo-Electron Tomography
title Structure and Assembly of the Proteus mirabilis Flagellar Motor by Cryo-Electron Tomography
title_full Structure and Assembly of the Proteus mirabilis Flagellar Motor by Cryo-Electron Tomography
title_fullStr Structure and Assembly of the Proteus mirabilis Flagellar Motor by Cryo-Electron Tomography
title_full_unstemmed Structure and Assembly of the Proteus mirabilis Flagellar Motor by Cryo-Electron Tomography
title_short Structure and Assembly of the Proteus mirabilis Flagellar Motor by Cryo-Electron Tomography
title_sort structure and assembly of the proteus mirabilis flagellar motor by cryo-electron tomography
topic Brief Report
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10179241/
https://www.ncbi.nlm.nih.gov/pubmed/37176000
http://dx.doi.org/10.3390/ijms24098292
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