4fhr

Crystal structure of the complex between the flagellar motor proteins FliG and FliM.

spinqualitylabelsall models 4fhr, resolution 1.93Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4fhr is a 2 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FLIM_THEMA FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheX chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity). Publication Abstract from PubMed The flagellar motor is one type of propulsion device of motile bacteria. The cytoplasmic ring (C-ring) of the motor interacts with the stator to generate torque in clockwise and counterclockwise directions. The C-ring is composed of three proteins, FliM, FliN, and FliG. Together they form the "switch complex" and regulate switching and torque generation. Here we report the crystal structure of the middle domain of FliM in complex with the middle and C-terminal domains of FliG that shows the interaction surface and orientations of the proteins. In the complex, FliG assumes a compact conformation in which the middle and C-terminal domains (FliG(MC)) collapse and stack together similarly to the recently published structure of a mutant of FliG(MC) with a clockwise rotational bias. This intramolecular stacking of the domains is distinct from the intermolecular stacking seen in other structures of FliG. We fit the complex structure into the three-dimensional reconstructions of the motor and propose that the cytoplasmic ring is assembled from 34 FliG and FliM molecules in a 1:1 fashion. Structure of flagellar motor proteins in complex allows for insights into motor structure and switching.,Vartanian AS, Paz A, Fortgang EA, Abramson J, Dahlquist FW J Biol Chem. 2012 Oct 19;287(43):35779-83. doi: 10.1074/jbc.C112.378380. Epub, 2012 Aug 15. PMID:22896702 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Flagellar protein 3D structures

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