3drk | pdb_00003drk

Crystal structure of Lactococcal OppA co-crystallized with Neuropeptide S in an open conformation

spinqualitylabelsall models 3drk, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3drk is a 2 chain structure with sequence from Laclm. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3drf, 3drg, 3drh, 3dri, 3drj Gene: oppA, llmg_0701 (LACLM) Resources: FirstGlance, OCA, RCSB, PDBsum 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 Oligopeptide-binding protein A (OppA) from Lactococcus lactis binds peptides of an exceptionally wide range of lengths (4-35 residues), with no apparent sequence preference. Here, we present the crystal structures of OppA in the open- and closed-liganded conformations. The structures directly explain the protein's phenomenal promiscuity. A huge cavity allows binding of very long peptides, and a lack of constraints for the position of the N and C termini of the ligand is compatible with binding of peptides with varying lengths. Unexpectedly, the peptide's amino-acid composition (but not the exact sequence) appears to have a function in selection, with a preference for proline-rich peptides containing at least one isoleucine. These properties can be related to the physiology of the organism: L. lactis is auxotrophic for branched chain amino acids and favours proline-rich caseins as a source of amino acids. We propose a new mechanism for peptide selection based on amino-acid composition rather than sequence. The structural basis for peptide selection by the transport receptor OppA.,Berntsson RP, Doeven MK, Fusetti F, Duurkens RH, Sengupta D, Marrink SJ, Thunnissen AM, Poolman B, Slotboom DJ EMBO J. 2009 Mar 19. PMID:19300437 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Oligopeptide-binding protein

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