5TDY

Structure of cofolded FliFc:FliGn complex from Thermotoga maritima

Summary for 5TDY

• Entry DOI: 10.2210/pdb5tdy/pdb
• Descriptor: Flagellar M-ring protein, Flagellar motor switch protein FliG (3 entities in total)
• Functional Keywords: flagellar motor, switch complex, motor protein
• Biological source: Thermotoga maritima; More
• Total number of polymer chains: 4
• Total formula weight: 32906.94

Authors

Lynch, M.J.,Levenson, R.,Kim, E.A.,Sircar, R.,Blair, D.F.,Dahlquist, F.W.,Crane, B.R. (deposition date: 2016-09-20, release date: 2017-01-25, Last modification date: 2024-11-20)

Primary citation

Lynch, M.J.,Levenson, R.,Kim, E.A.,Sircar, R.,Blair, D.F.,Dahlquist, F.W.,Crane, B.R.
Co-Folding of a FliF-FliG Split Domain Forms the Basis of the MS:C Ring Interface within the Bacterial Flagellar Motor.
Structure, 25:317-328, 2017

PubMed Abstract: The interface between the membrane (MS) and cytoplasmic (C) rings of the bacterial flagellar motor couples torque generation to rotation within the membrane. The structure of the C-terminal helices of the integral membrane protein FliF (FliF) bound to the N terminal domain of the switch complex protein FliG (FliG) reveals that FliG folds around FliF to produce a topology that closely resembles both the middle and C-terminal domains of FliG. The interface is consistent with solution-state nuclear magnetic resonance, small-angle X-ray scattering, in vivo interaction studies, and cellular motility assays. Co-folding with FliF induces substantial conformational changes in FliG and suggests that FliF and FliG have the same stoichiometry within the rotor. Modeling the FliF:FliG complex into cryo-electron microscopy rotor density updates the architecture of the middle and upper switch complex and shows how domain shuffling of a conserved interaction module anchors the cytoplasmic rotor to the membrane.

PubMed: 28089452
DOI: 10.1016/j.str.2016.12.006

Experimental method

X-RAY DIFFRACTION (2.105 Å)