5TDY

Structure of cofolded FliFc:FliGn complex from Thermotoga maritima

5TDY の概要

• エントリーDOI: 10.2210/pdb5tdy/pdb
• 分子名称: Flagellar M-ring protein, Flagellar motor switch protein FliG (3 entities in total)
• 機能のキーワード: flagellar motor, switch complex, motor protein
• 由来する生物種: Thermotoga maritima; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 32906.94

構造登録者

Lynch, M.J.,Levenson, R.,Kim, E.A.,Sircar, R.,Blair, D.F.,Dahlquist, F.W.,Crane, B.R. (登録日: 2016-09-20, 公開日: 2017-01-25, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.105 Å)