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Acta Crystallogr D Biol Crystallogr. 2011 Dec;67(Pt 12):1009-16. doi: 10.1107/S0907444911041102. Epub 2011 Nov 5.

Role of the MotB linker in the assembly and activation of the bacterial flagellar motor.

Author information

1
Manchester Interdisciplinary Biocentre, University of Manchester, 131 Princess Street, Manchester M1 7DN, England.

Abstract

Bacterial flagella are driven by an ion influx through the peptidoglycan (PG)-tethered MotA/MotB stator. Stator precomplexes assemble in the membrane and remain inactive until they incorporate into the motor, upon which MotA/MotB changes conformation. The nature of this change and the mechanism of inhibition of the PG-binding and ion-conducting activities of the precomplexes are unknown. Here, the structural analysis of a series of N-terminally truncated MotB fragments is presented, the mechanism of inhibition by the linker is identified and the structural basis for the formation of the PG-binding-competent open-channel MotA/MotB conformation via a mechanism that entails linker unfolding and rotational displacement of MotB transmembrane helices is uncovered.

PMID:
22120737
DOI:
10.1107/S0907444911041102
[Indexed for MEDLINE]

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