6YSF

Structure of the flagellar MotAB stator complex from Clostridium sporogenes

Summary for 6YSF

• Entry DOI: 10.2210/pdb6ysf/pdb
• EMDB information: 10895
• Descriptor: Chemotaxis motB protein, Chemotaxis MotA protein (2 entities in total)
• Functional Keywords: stator flagellar rotation ion driven motor, motor protein
• Biological source: Clostridium sporogenes; More
• Total number of polymer chains: 7
• Total formula weight: 203964.62

Authors

Lea, S.M.,Deme, J.C.,Johnson, S.J. (deposition date: 2020-04-22, release date: 2020-08-12, Last modification date: 2024-05-22)

Primary citation

Deme, J.C.,Johnson, S.,Vickery, O.,Aron, A.,Monkhouse, H.,Griffiths, T.,James, R.H.,Berks, B.C.,Coulton, J.W.,Stansfeld, P.J.,Lea, S.M.
Structures of the stator complex that drives rotation of the bacterial flagellum.
Nat Microbiol, 5:1553-1564, 2020

PubMed 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 AB subunit assembly where the five A subunits enclose the two B subunits. Comparison to structures of other ion-driven motors indicates that this AB 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.

PubMed: 32929189
DOI: 10.1038/s41564-020-0788-8

Experimental method

ELECTRON MICROSCOPY (3.4 Å)