3S02

The crystal structure of the periplasmic domain of Helicobacter pylori MotB (residues 103-256)

Summary for 3S02

• Entry DOI: 10.2210/pdb3s02/pdb
• Related: 3S03 3S06 3S0H 3S0W 3S0Y
• Descriptor: Motility protein B (2 entities in total)
• Functional Keywords: peptidoglycan binding, flagellar rotation, chemotaxis, bacterial flagellar motor, membrane, motor protein
• Biological source: Helicobacter pylori
• Cellular location: Cell inner membrane (By similarity); Single- pass type II membrane protein (Potential): P56427
• Total number of polymer chains: 2
• Total formula weight: 35205.79

Authors

Roujeinikova, A.R. (deposition date: 2011-05-12, release date: 2012-03-14, Last modification date: 2024-02-28)

Primary citation

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.,Sect.D, 67:1009-1016, 2011

PubMed 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.

PubMed: 22120737
DOI: 10.1107/S0907444911041102

Experimental method

X-RAY DIFFRACTION (2.5 Å)