Nat Microbiol
Sir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Published: February 2021
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.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7116788 | PMC |
http://dx.doi.org/10.1038/s41564-020-00823-6 | DOI Listing |
Nature
December 2024
Structural Biology of Molecular Machines Group, Protein Structure & Function Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
Zorya is a recently identified and widely distributed bacterial immune system that protects bacteria from viral (phage) infections. Three Zorya subtypes have been discovered, each containing predicted membrane-embedded ZorAB complexes paired with soluble subunits that differ among Zorya subtypes, notably ZorC and ZorD in type I Zorya systems. Here, we investigate the molecular basis of Zorya defense using cryo-electron microscopy, mutagenesis, fluorescence microscopy, proteomics, and functional studies.
View Article and Find Full Text PDFBMC Microbiol
November 2024
Hefei National Research Center for Physical Sciences at the Microscale and Department of Physics, University of Science and Technology of China, Hefei, Anhui, 230026, China.
MotY homologs are present in a variety of monotrichous bacterial strains and are thought to form an additional structural T ring in flagellar motors. While MotY potentially plays an important role in motor torque generation, its impact on motor output dynamics remains poorly understood. In this study, we investigate the role of MotY in P.
View Article and Find Full Text PDFBiophys J
July 2023
Department of Biophysics, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan. Electronic address:
FF ATP synthase, a ubiquitous enzyme that synthesizes most ATP in living cells, is composed of two rotary motors: a membrane-embedded proton-driven F motor and a catalytic F motor. These motors share both central and peripheral stalks. Although both F and F have pseudo-symmetric structures, their symmetries do not match.
View Article and Find Full Text PDFFront Microbiol
March 2021
Department of Life Sciences, Imperial College London, London, United Kingdom.
The γ-proteobacteria are a group of diverse bacteria including pathogenic , and species. The majority swim in liquids with polar, sodium-driven flagella and swarm on surfaces with lateral, non-chemotactic flagella. Notable exceptions are the enteric Enterobacteriaceae such as and .
View Article and Find Full Text PDFNat Microbiol
February 2021
Sir William Dunn School of Pathology, University of Oxford, Oxford, UK.
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.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!
© LitMetric 2025. All rights reserved.