EMD-10895

Single-particle
3.4 Å
EMD-10895 Deposition: 22/04/2020
Map released: 12/08/2020
Last modified: 22/05/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-10895

Structure of the flagellar MotAB stator complex from Clostridium sporogenes

EMD-10895

Single-particle
3.4 Å
EMD-10895 Deposition: 22/04/2020
Map released: 12/08/2020
Last modified: 22/05/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Clostridium sporogenes
Sample: MotAB
Fitted models: 6ysf (Avg. Q-score: 0.449)

Deposition Authors: Lea SM , Deme JC
Structures of the stator complex that drives rotation of the bacterial flagellum.
Deme JC , Johnson S , Vickery O , Aron A, Monkhouse H, Griffiths T , James RH, Berks BC, Coulton JW, Stansfeld PJ, Lea SM
(2020) Nat Microbiol , 5 , 1553 - 1564
PUBMED: 32929189
DOI: doi:10.1038/s41564-020-0788-8
ISSN: 2058-5276
Abstract:
The bacterial flagellum is the prototypical protein nanomachine and comprises a rotating helical propeller attached to a membrane-embedded motor complex. The motor consists of a central rotor surrounded by stator units that couple ion flow across the cytoplasmic membrane to generate torque. Here, we present the structures of the stator complexes from Clostridium sporogenes, Bacillus subtilis and Vibrio mimicus, allowing interpretation of the extensive body of data on stator mechanism. The structures reveal an unexpected asymmetric A5B2 subunit assembly where the five A subunits enclose the two B subunits. Comparison to structures of other ion-driven motors indicates that this A5B2 architecture is fundamental to bacterial systems that couple energy from ion flow to generate mechanical work at a distance and suggests that such events involve rotation in the motor structures.