3S0Y: The Crystal Structure Of The Periplasmic Domain Of Motb (Residues 64- 256)

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.
PDB ID: 3S0YDownload
MMDB ID: 97931
PDB Deposition Date: 2011/5/13
Updated in MMDB: 2012/03
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 3S0Y: dimeric; determined by author and by software (PISA)
Molecular Components in 3S0Y
Label Count Molecule
Proteins (2 molecules)
Motility Protein B(Gene symbol: motB)
Molecule annotation
Chemicals (3 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB