4fq0 | pdb_00004fq0

Crystal structure of FliG-FliM complex from H. pylori

spinqualitylabelsall models 4fq0, resolution 2.82Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4fq0 is a 4 chain structure with sequence from Campylobacter pylori. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3usw, 3usy Gene: FliM (Campylobacter pylori), FliG (Campylobacter pylori) 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 FliG and FliM are switch proteins that regulate the rotation and switching of the flagellar motor. Several assembly models for FliG and FliM have recently been proposed; however, it remains unclear whether the assembly of the switch proteins is conserved among different bacterial species. We applied a combination of pull-down, thermodynamic and structural analyses to characterize the FliM-FliG association from the mesophilic bacterium Helicobacter pylori. FliM binds to FliG with micromolar binding affinity, and their interaction is mediated through the middle domain of FliG (FliGM ), which contains the EHPQR motif. Crystal structures of the middle domain of H. pylori FliM (FliMM ) and FliGM -FliMM complex revealed that FliG binding triggered a conformational change of the FliM alpha3-alpha1' loop, especially Asp130 and Arg144. We furthermore showed that various highly conserved residues in this region are required for FliM-FliG complex formation. Although the FliM-FliG complex structure displayed a conserved binding mode when compared with Thermotoga maritima, variable residues were identified that may contribute to differential binding affinities across bacterial species. Comparison of the thermodynamic parameters of FliG-FliM interactions between H. pylori and Escherichia coli suggests that molecular basis and binding properties of FliM to FliG is likely different between these two species. Structural basis of FliG-FliM interaction in Helicobacter pylori.,Lam KH, Lam WW, Wong JY, Chan LC, Kotaka M, Ling TK, Jin DY, Ottemann KM, Au SW Mol Microbiol. 2013 Apr 24. doi: 10.1111/mmi.12222. PMID:23614777 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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