8arn | pdb_00008arn

Crystal structure of the peptide binding protein, OppA, from Bacillus subtilis in complex with an endogenous tetrapeptide

spinqualitylabelsall models 8arn, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8arn is a 4 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168 and Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function OPPA_BACSU This protein is a component of the oligopeptide permease, a binding protein-dependent transport system, It binds peptides up to five amino acids long with high affinity. Also required for sporulation and competence. Publication Abstract from PubMed Peptide transporters play important nutritional and cell signalling roles in Bacillus subtilis, which are pronounced during stationary phase adaptations and development. Three high-affinity ATP-binding cassette (ABC) family transporters are involved in peptide uptake - the oligopeptide permease (Opp), another peptide permease (App) and a less well-characterized dipeptide permease (Dpp). Here we report crystal structures of the extracellular substrate binding proteins, OppA and DppE, which serve the Opp and Dpp systems, respectively. The structure of OppA was determined in complex with endogenous peptides, modelled as Ser-Asn-Ser-Ser, and with the sporulation-promoting peptide Ser-Arg-Asn-Val-Thr, which bind with K (d) values of 0.4 and 2 microM, respectively, as measured by isothermal titration calorimetry. Differential scanning fluorescence experiments with a wider panel of ligands showed that OppA has highest affinity for tetra- and penta-peptides. The structure of DppE revealed the unexpected presence of a murein tripeptide (MTP) ligand, l-Ala-d-Glu-meso-DAP, in the peptide binding groove. The mode of MTP binding in DppE is different to that observed in the murein peptide binding protein, MppA, from Escherichia coli, suggesting independent evolution of these proteins from an OppA-like precursor. The presence of MTP in DppE points to a role for Dpp in the uptake and recycling of cell wall peptides, a conclusion that is supported by analysis of the genomic context of dpp, which revealed adjacent genes encoding enzymes involved in muropeptide catabolism in a gene organization that is widely conserved in Firmicutes. Peptide transport in Bacillus subtilis - structure and specificity in the extracellular solute binding proteins OppA and DppE.,Hughes AM, Darby JF, Dodson EJ, Wilson SJ, Turkenburg JP, Thomas GH, Wilkinson AJ Microbiology (Reading). 2022 Dec;168(12). doi: 10.1099/mic.0.001274. PMID:36748525 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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