Characterization of C-ring component assembly in flagellar motors from amino acid coevolution
Journal Article
·
· Royal Society Open Science
- Univ. of Campinas (UNICAMP), Sao Paulo (Brazil). Inst. of Chemistry and Center for Computational Engineering and Science; DOE/OSTI
- Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Molecular Foundry. Molecular Biology Consortium
- 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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