2w8b | pdb_00002w8b

Crystal structure of processed TolB in complex with Pal

spinqualitylabelsall models 2w8b, resolution 1.86Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2w8b is a 8 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.86Å Ligands: ACT, GOL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TOLB_ECOLI Involved in the TonB-independent uptake of group A colicins (colicins A, E1, E2, E3 and K). Necessary for the colicins to reach their respective targets after initial binding to the bacteria.[HAMAP-Rule:MF_00671] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The Tol system is a five-protein assembly parasitized by colicins and bacteriophages that helps stabilize the Gram-negative outer membrane (OM). We show that allosteric signalling through the six-bladed beta-propeller protein TolB is central to Tol function in Escherichia coli and that this is subverted by colicins such as ColE9 to initiate their OM translocation. Protein-protein interactions with the TolB beta-propeller govern two conformational states that are adopted by the distal N-terminal 12 residues of TolB that bind TolA in the inner membrane. ColE9 promotes disorder of this 'TolA box' and recruitment of TolA. In contrast to ColE9, binding of the OM lipoprotein Pal to the same site induces conformational changes that sequester the TolA box to the TolB surface in which it exhibits little or no TolA binding. Our data suggest that Pal is an OFF switch for the Tol assembly, whereas colicins promote an ON state even though mimicking Pal. Comparison of the TolB mechanism to that of vertebrate guanine nucleotide exchange factor RCC1 suggests that allosteric signalling may be more prevalent in beta-propeller proteins than currently realized. Allosteric beta-propeller signalling in TolB and its manipulation by translocating colicins.,Bonsor DA, Hecht O, Vankemmelbeke M, Sharma A, Krachler AM, Housden NG, Lilly KJ, James R, Moore GR, Kleanthous C EMBO J. 2009 Sep 16;28(18):2846-57. Epub 2009 Aug 20. PMID:19696740 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pal TolB

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