@article{42fe83c78fdd454f846cf46156446113,
title = "Structure and mechanism of the proton-driven motor that powers type 9 secretion and gliding motility",
abstract = "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.",
author = "{Hennell James}, Rory and Deme, {Justin C} and Andreas Kjӕr and Felicity Alcock and Augustinas Silale and Frederic LAUBER and Steven Johnson and Berks, {Ben C} and Lea, {Susan M}",
note = "Funding Information: We thank M. McBride and Y. Zhu for providing reagents for the genetic manipulation of F. johnsoniae. We thank L. Lavis for supplying the Janelia Fluor ligands, S. Hickman for advice on fluorescence imaging and A. Wainman for assistance with phase contrast imaging. We thank P. Guy for his involvement in producing the pulse-chase mCherry–CTD fusion construct and R. Berry for discussions. We acknowledge the use of the Central Oxford Structural Microscopy and Imaging Centre (COSMIC) and the Oxford Micron Advanced Imaging Facility. We thank K. Foster for providing additional imaging facilities. This work was supported by Wellcome Trust studentships to R.H.J. and A.S. (grant no. 1009136), a Biotechnology and Biological Sciences Research Council studentship to A.K. and Wellcome Trust Investigator Awards (grant nos. 107929/Z/15/Z and 100298/Z/12/Z). COSMIC was supported by a Wellcome Trust Collaborative Award (grant no. 201536/Z/16/Z), the Wolfson Foundation, a Royal Society Wolfson Refurbishment Grant, the John Fell Fund, and the EPA and Cephalosporin Trusts. Publisher Copyright: {\textcopyright} 2021, The Author(s), under exclusive licence to Springer Nature Limited.",
year = "2021",
month = feb,
doi = "10.1038/s41564-020-00823-6",
language = "English",
volume = "6",
pages = "221--233",
journal = "Nature Microbiology",
issn = "2058-5276",
publisher = "Nature Publishing Group",
number = "2",
}