3s0w | pdb_00003s0w

The crystal structure of the periplasmic domain of Helicobacter pylori MotB (residues 78-256).

spinqualitylabelsall models 3s0w, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3s0w is a 2 chain structure with sequence from Campylobacter pylori. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 Related: 3s02, 3s03, 3s06, 3s0h, 3s0y Gene: HP_0816, motB (Campylobacter pylori) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MOTB_HELPY] MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Might be a linker that fastens the torque-generating machinery to the cell wall (By similarity). Publication Abstract from PubMed 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chemotaxis protein 3D structures

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