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Characterization of C-ring component assembly in flagellar motors from amino acid coevolution

Journal Article · · Royal Society Open Science
DOI:https://doi.org/10.1098/rsos.171854· OSTI ID:1625593
 [1];  [2];  [3]
  1. Univ. of Campinas (UNICAMP), Sao Paulo (Brazil). Inst. of Chemistry and Center for Computational Engineering and Science; DOE/OSTI
  2. Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Molecular Foundry. Molecular Biology Consortium
  3. Univ. of Texas at Dallas, Richardson, TX (United States). Dept. of Biological Sciences. Dept. of Bioengineering. Center for Systems Biology
Bacterial flagellar motility, an important virulence factor, is energized by a rotary motor localized within the flagellar basal body. The rotor module consists of a large framework (the C-ring), composed of the FliG, FliM and FliN proteins. FliN and FliM contacts the FliG torque ring to control the direction of flagellar rotation. We report that structure-based models constrained only by residue coevolution can recover the binding interface of atomic X-ray dimer complexes with remarkable accuracy (approx. 1 Å RMSD). We propose a model for FliM–FliN heterodimerization, which agrees accurately with homologous interfaces as well as in situ cross-linking experiments, and hence supports a proposed architecture for the lower portion of the C-ring. Furthermore, this approach allowed the identification of two discrete and interchangeable homodimerization interfaces between FliM middle domains that agree with experimental measurements and might be associated with C-ring directional switching dynamics triggered upon binding of CheY signal protein. Our findings provide structural details of complex formation at the C-ring that have been difficult to obtain with previous methodologies and clarify the architectural principle that underpins the ultra-sensitive allostery exhibited by this ring assembly that controls the clockwise or counterclockwise rotation of flagella.
Research Organization:
Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
Sponsoring Organization:
USDOE Office of Science (SC)
Grant/Contract Number:
AC02-05CH11231
OSTI ID:
1625593
Journal Information:
Royal Society Open Science, Journal Name: Royal Society Open Science Journal Issue: 5 Vol. 5; ISSN 2054-5703
Publisher:
The Royal Society PublishingCopyright Statement
Country of Publication:
United States
Language:
English

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