3SOH

Architecture of the Flagellar Rotor

Summary for 3SOH

• Entry DOI: 10.2210/pdb3soh/pdb
• Related: 1LKV 2HP7
• Descriptor: Flagellar motor switch protein FliM, Flagellar motor switch protein FliG (3 entities in total)
• Functional Keywords: protein-protein complex, alpha/beta, motor protein
• Biological source: Thermotoga maritima; More
• Cellular location: Cell inner membrane ; Peripheral membrane protein : Q9WZE6; Cell inner membrane ; Peripheral membrane protein ; Cytoplasmic side : Q9WY63
• Total number of polymer chains: 4
• Total formula weight: 61496.69

Authors

Koushik, P.,Gonzalez-Bonet, G.,Bilwes, A.M.,Crane, B.R.,Blair, D. (deposition date: 2011-06-30, release date: 2011-07-27, Last modification date: 2023-09-13)

Primary citation

Paul, K.,Gonzalez-Bonet, G.,Bilwes, A.M.,Crane, B.R.,Blair, D.
Architecture of the flagellar rotor.
Embo J., 30:2962-2971, 2011

PubMed Abstract: Rotation and switching of the bacterial flagellum depends on a large rotor-mounted protein assembly composed of the proteins FliG, FliM and FliN, with FliG most directly involved in rotation. The crystal structure of a complex between the central domains of FliG and FliM, in conjunction with several biochemical and molecular-genetic experiments, reveals the arrangement of the FliG and FliM proteins in the rotor. A stoichiometric mismatch between FliG (26 subunits) and FliM (34 subunits) is explained in terms of two distinct positions for FliM: one where it binds the FliG central domain and another where it binds the FliG C-terminal domain. This architecture provides a structural framework for addressing the mechanisms of motor rotation and direction switching and for unifying the large body of data on motor performance. Recently proposed alternative models of rotor assembly, based on a subunit contact observed in crystals, are not supported by experiment.

PubMed: 21673656
DOI: 10.1038/emboj.2011.188

Experimental method

X-RAY DIFFRACTION (3.5 Å)