3usw

Crystal structure of FliG (residues 86-343) from H. pylori

spinqualitylabelsall models 3usw, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3usw is a 1 chain structure with sequence from Helicobacter pylori. This structure supersedes the now removed PDB entry 3pkr. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.601Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FLIG_HELPY One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation. Required for flagellum synthesis and motility. In H.pylori four flagellar switch proteins are encoded, FliG, FliM, FliN and FliY. Publication Abstract from PubMed Bacterial flagellar switching between counterclockwise and clockwise directions is mediated by the coupling of the chemotactic system and the motor switch complex. The conformational changes of FliG are closely associated with this switching mechanism. We present two crystal structures of FliG(MC) from Helicobacter pylori, each showing distinct domain orientations from previously solved structures. A 180 degrees rotation of the charged ridge-containing C-terminal subdomain FliG(Calpha1-6) that is prompted by the rotational freedom of Met245 psi and Phe246 phi at the MFXF motif was revealed. Studies on the swarming and swimming behavior of Escherichia coli mutants further identified the importance of the (2)(4)(5)MFXF(2)(4)(8) motif and a highly conserved residue, Asn216, in motor switching. Additionally, multiple conformations of FliG(Calpha1-6) were demonstrated by intramolecular cysteine crosslinking. The conformational flexibility of FliGc leads us to propose a model that accounts for the symmetrical torque generation process and for the dynamics of the motor. Multiple conformations of the FliG C-terminal domain provide insight into flagellar motor switching.,Lam KH, Ip WS, Lam YW, Chan SO, Ling TK, Au SW Structure. 2012 Feb 8;20(2):315-25. PMID:22325779 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Flagellar protein 3D structures

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