3b0z | pdb_00003b0z

Crystal structure of cytoplasmic domain of FlhB from Salmonella typhimurium

spinqualitylabelsall models 3b0z, resolution 2.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3b0z is a 2 chain structure with sequence from "bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NA, ZN Related: 3b1s Gene: flhB ("Bacillus typhimurium" Loeffler 1892) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FLHB_SALTY] Required for formation of the rod structure in the basal body of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin. Publication Abstract from PubMed The membrane protein FlhB is a highly conserved component of the flagellar secretion system. It is composed of an N-terminal transmembrane domain and a C-terminal cytoplasmic domain (FlhBC). Here, the crystal structures of FlhBC from Salmonella typhimurium and Aquifex aeolicus are described at 2.45 and 2.55 A resolution, respectively. These flagellar FlhBC structures are similar to those of paralogues from the needle type III secretion system, with the major difference being in a linker that connects the transmembrane and cytoplasmic domains of FlhB. It was found that deletion of a short flexible loop in a globular part of Salmonella FlhBC leads to complete inhibition of secretion by the flagellar secretion system. Molecular-dynamics calculations demonstrate that the linker region is the most flexible part of FlhBC and that the deletion of the loop reduces this flexibility. These results are in good agreement with previous studies showing the importance of the linker in the function of FlhB and provide new insight into the relationship between the different parts of the FlhBC molecule. Inhibition of a type III secretion system by the deletion of a short loop in one of its membrane proteins.,Meshcheryakov VA, Kitao A, Matsunami H, Samatey FA Acta Crystallogr D Biol Crystallogr. 2013 May;69(Pt 5):812-20. doi:, 10.1107/S0907444913002102. Epub 2013 Apr 11. PMID:23633590 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Fadel A. Samatey Group User:Fadel A. Samatey/FlhBc I

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