3s0h is a 4 chain structure with sequence from Helicobacter pylori. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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.
Role of the MotB linker in the assembly and activation of the bacterial flagellar motor.,O'Neill J, Xie M, Hijnen M, Roujeinikova A Acta Crystallogr D Biol Crystallogr. 2011 Dec;67(Pt 12):1009-16. Epub 2011 Nov 5. PMID:22120737[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ O'Neill J, Xie M, Hijnen M, Roujeinikova A. Role of the MotB linker in the assembly and activation of the bacterial flagellar motor. Acta Crystallogr D Biol Crystallogr. 2011 Dec;67(Pt 12):1009-16. Epub 2011 Nov 5. PMID:22120737 doi:10.1107/S0907444911041102
