6i3g | pdb_00006i3g

Crystal structure of a putative peptide binding protein AppA from Clostridium difficile

spinqualitylabelsall models 6i3g, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6i3g is a 1 chain structure with sequence from "bacillus_difficilis"_hall_and_o'toole_1935 "bacillus difficilis" hall and o'toole 1935. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: IOD, SO4 Gene: appA, appA_1, BGU81_05565, BN1095_250054, BN1096_520027, BN1097_680156, SAMEA3374989_00890 ("Bacillus difficilis" Hall and O'Toole 1935) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Peptides play an important signalling role in Bacillus subtilis, where their uptake by one of two ABC-type oligopeptide transporters, Opp and App, is required for efficient sporulation. Homologues of these transporters in Clostridium difficile have been characterized, but their role, and hence that of peptides, in regulating sporulation in this organism is less clear. Here, the oligopeptide-binding receptor proteins for these transporters, CdAppA and CdOppA, have been purified and partially characterized, and the crystal structure of CdAppA has been determined in an open unliganded form. Peptide binding to either protein could not be observed in Thermofluor assays with a set of ten peptides of varying lengths and compositions. Re-examination of the protein sequences together with structure comparisons prompts the proposal that CdAppA is not a versatile peptide-binding protein but instead may bind a restricted set of peptides. Meanwhile, CdOppA is likely to be the receptor protein for a nickel-uptake system. Crystal structure of the putative peptide-binding protein AppA from Clostridium difficile.,Hughes A, Wilson S, Dodson EJ, Turkenburg JP, Wilkinson AJ Acta Crystallogr F Struct Biol Commun. 2019 Apr 1;75(Pt 4):246-253. doi:, 10.1107/S2053230X1900178X. Epub 2019 Mar 13. PMID:30950825 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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