A coevolution-guided model for the rotor of the bacterial flagellar motor
Abstract
The Salmonella typhimurium trans-membrane FliF MS ring templates assembly of the rotary bacterial fagellar motor, which also contains a cytoplasmic C-ring. A full-frame fusion of FliF with the rotor protein FliG assembles rings in non-motile expression hosts. 3D electron microscopy reconstructions of these FliFFliG rings show three high electron-density sub-volumes. 3D-classifcation revealed heterogeneity of the assigned cytoplasmic volume consistent with FliG lability. We used residue coevolution to construct homodimer building blocks for ring assembly, with X-ray crystal structures from other species and injectisome analogs. The coevolution signal validates folds and, importantly, indicates strong homodimer contacts for three ring building motifs (RBMs), initially identified in injectisome structures. It also indicates that the cofolded domains of the FliG N-terminal domain (FliG_N) with embedded α-helical FliF carboxy-terminal tail homo-oligomerize. The FliG middle and C-terminal domains (FliG_MC) have a weak signal for homo-dimerization but have coevolved to conserve their stacking contact. The homodimers and their ring models ft well into the 3D reconstruction. We hypothesize that a stable FliF periplasmic hub provides a platform for FliG ring self-assembly, but the FliG_MC ring has only limited stability without the C-ring. We also present a mechanical model for torque transmission in the FliFFliG ring.
- Authors:
-
- National Institutes of Health (NIH), Bethesda, MD (United States). Center for Cancer Research. Lab. of Cell Biology; Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Molecular Biology Consortium
- National Institutes of Health (NIH), Bethesda, MD (United States). Center for Cancer Research. Lab. of Cell Biology
- Publication Date:
- Research Org.:
- Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division
- OSTI Identifier:
- 1624413
- Grant/Contract Number:
- AC02-05CH11231
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Scientific Reports
- Additional Journal Information:
- Journal Volume: 8; Journal Issue: 1; Journal ID: ISSN 2045-2322
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; Science & Technology - Other Topics
Citation Formats
Khan, Shahid, Guo, Tai Wei, and Misra, Saurav. A coevolution-guided model for the rotor of the bacterial flagellar motor. United States: N. p., 2018.
Web. doi:10.1038/s41598-018-30293-0.
Khan, Shahid, Guo, Tai Wei, & Misra, Saurav. A coevolution-guided model for the rotor of the bacterial flagellar motor. United States. https://doi.org/10.1038/s41598-018-30293-0
Khan, Shahid, Guo, Tai Wei, and Misra, Saurav. Mon .
"A coevolution-guided model for the rotor of the bacterial flagellar motor". United States. https://doi.org/10.1038/s41598-018-30293-0. https://www.osti.gov/servlets/purl/1624413.
@article{osti_1624413,
title = {A coevolution-guided model for the rotor of the bacterial flagellar motor},
author = {Khan, Shahid and Guo, Tai Wei and Misra, Saurav},
abstractNote = {The Salmonella typhimurium trans-membrane FliF MS ring templates assembly of the rotary bacterial fagellar motor, which also contains a cytoplasmic C-ring. A full-frame fusion of FliF with the rotor protein FliG assembles rings in non-motile expression hosts. 3D electron microscopy reconstructions of these FliFFliG rings show three high electron-density sub-volumes. 3D-classifcation revealed heterogeneity of the assigned cytoplasmic volume consistent with FliG lability. We used residue coevolution to construct homodimer building blocks for ring assembly, with X-ray crystal structures from other species and injectisome analogs. The coevolution signal validates folds and, importantly, indicates strong homodimer contacts for three ring building motifs (RBMs), initially identified in injectisome structures. It also indicates that the cofolded domains of the FliG N-terminal domain (FliG_N) with embedded α-helical FliF carboxy-terminal tail homo-oligomerize. The FliG middle and C-terminal domains (FliG_MC) have a weak signal for homo-dimerization but have coevolved to conserve their stacking contact. The homodimers and their ring models ft well into the 3D reconstruction. We hypothesize that a stable FliF periplasmic hub provides a platform for FliG ring self-assembly, but the FliG_MC ring has only limited stability without the C-ring. We also present a mechanical model for torque transmission in the FliFFliG ring.},
doi = {10.1038/s41598-018-30293-0},
journal = {Scientific Reports},
number = 1,
volume = 8,
place = {United States},
year = {Mon Aug 06 00:00:00 EDT 2018},
month = {Mon Aug 06 00:00:00 EDT 2018}
}
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Cd-hit: a fast program for clustering and comparing large sets of protein or nucleotide sequences
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ZDOCK server: interactive docking prediction of protein-protein complexes and symmetric multimers
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Structural basis of FliG-FliM interaction in Helicobacter pylori: FliG-FliM interaction in Helicobacter pylori
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Conformational Spread as a Mechanism for Cooperativity in the Bacterial Flagellar Switch
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