5wrh | pdb_00005wrh

FlgG structure based on the CryoEM map of the bacterial flagellar polyrod

Loading... Status: waiting for Mol* initialization Structural highlights 5wrh is a 1 chain structure with sequence from Salty. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The bacterial flagellum is a motile organelle driven by a rotary motor, and its axial portions function as a drive shaft (rod), a universal joint (hook) and a helical propeller (filament). The rod and hook are directly connected to each other, with their subunit proteins FlgG and FlgE having 39% sequence identity, but show distinct mechanical properties; the rod is straight and rigid as a drive shaft whereas the hook is flexible in bending as a universal joint. Here we report the structure of the rod and comparison with that of the hook. While these two structures have the same helical symmetry and repeat distance and nearly identical folds of corresponding domains, the domain orientations differ by approximately 7 degrees , resulting in tight and loose axial subunit packing in the rod and hook, respectively, conferring the rigidity on the rod and flexibility on the hook. This provides a good example of versatile use of a protein structure in biological organisms. Identical folds used for distinct mechanical functions of the bacterial flagellar rod and hook.,Fujii T, Kato T, Hiraoka KD, Miyata T, Minamino T, Chevance FF, Hughes KT, Namba K Nat Commun. 2017 Jan 25;8:14276. doi: 10.1038/ncomms14276. PMID:28120828 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Flagellar protein 3D structures User:Fadel A. Samatey/FlgE III/Intrinsically Disordered Flagellar Rod Stretch

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