Structure and mechanism of the proton-driven motor that powers Type 9 secretion and gliding motility

Three classes of ion-driven protein motors have been identified to date: ATP synthase, the bacterial flagellar motor and a proton-driven motor that powers gliding motility and the type 9 protein secretion system in Bacteroidetes bacteria. Here, we present cryo-electron microscopy structures of the g...

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Asıl Yazarlar: Hennell James, R, Deme, JC, Kjaer, A, Alcock, F, Silale, A, Lauber, F, Johnson, S, Berks, B, Lea, SM
Materyal Türü: Journal article
Dil:English
Baskı/Yayın Bilgisi: Springer Nature 2021
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author Hennell James, R
Deme, JC
Kjaer, A
Alcock, F
Silale, A
Lauber, F
Johnson, S
Berks, B
Lea, SM
author_facet Hennell James, R
Deme, JC
Kjaer, A
Alcock, F
Silale, A
Lauber, F
Johnson, S
Berks, B
Lea, SM
author_sort Hennell James, R
collection OXFORD
description Three classes of ion-driven protein motors have been identified to date: ATP synthase, the bacterial flagellar motor and a proton-driven motor that powers gliding motility and the type 9 protein secretion system in Bacteroidetes bacteria. Here, we present cryo-electron microscopy structures of the gliding motility/type 9 protein secretion system motors GldLM from Flavobacterium johnsoniae and PorLM from Porphyromonas gingivalis. The motor is an asymmetric inner membrane protein complex in which the single transmembrane helices of two periplasm-spanning GldM/PorM proteins are positioned inside a ring of five GldL/PorL proteins. Mutagenesis and single-molecule tracking identify protonatable amino acid residues in the transmembrane domain of the complex that are important for motor function. Our data provide evidence for a mechanism in which proton flow results in rotation of the periplasm-spanning GldM/PorM dimer inside the intra-membrane GldL/PorL ring to drive processes at the bacterial outer membrane.
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spelling oxford-uuid:07f0ad43-3221-4b8d-b537-25dc5e0b8db12022-03-26T09:10:16ZStructure and mechanism of the proton-driven motor that powers Type 9 secretion and gliding motilityJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:07f0ad43-3221-4b8d-b537-25dc5e0b8db1EnglishSymplectic ElementsSpringer Nature2021Hennell James, RDeme, JCKjaer, AAlcock, FSilale, ALauber, FJohnson, SBerks, BLea, SMThree classes of ion-driven protein motors have been identified to date: ATP synthase, the bacterial flagellar motor and a proton-driven motor that powers gliding motility and the type 9 protein secretion system in Bacteroidetes bacteria. Here, we present cryo-electron microscopy structures of the gliding motility/type 9 protein secretion system motors GldLM from Flavobacterium johnsoniae and PorLM from Porphyromonas gingivalis. The motor is an asymmetric inner membrane protein complex in which the single transmembrane helices of two periplasm-spanning GldM/PorM proteins are positioned inside a ring of five GldL/PorL proteins. Mutagenesis and single-molecule tracking identify protonatable amino acid residues in the transmembrane domain of the complex that are important for motor function. Our data provide evidence for a mechanism in which proton flow results in rotation of the periplasm-spanning GldM/PorM dimer inside the intra-membrane GldL/PorL ring to drive processes at the bacterial outer membrane.
spellingShingle Hennell James, R
Deme, JC
Kjaer, A
Alcock, F
Silale, A
Lauber, F
Johnson, S
Berks, B
Lea, SM
Structure and mechanism of the proton-driven motor that powers Type 9 secretion and gliding motility
title Structure and mechanism of the proton-driven motor that powers Type 9 secretion and gliding motility
title_full Structure and mechanism of the proton-driven motor that powers Type 9 secretion and gliding motility
title_fullStr Structure and mechanism of the proton-driven motor that powers Type 9 secretion and gliding motility
title_full_unstemmed Structure and mechanism of the proton-driven motor that powers Type 9 secretion and gliding motility
title_short Structure and mechanism of the proton-driven motor that powers Type 9 secretion and gliding motility
title_sort structure and mechanism of the proton driven motor that powers type 9 secretion and gliding motility
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