Journal
EMBO JOURNAL
Volume 28, Issue 9, Pages 1332-1340Publisher
WILEY
DOI: 10.1038/emboj.2009.65
Keywords
mass spectrometry; peptide binding; peptide transport; X-ray crystallography
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Funding
- Marie Curie Early Stage Training
- Netherlands Organisation for Scientific Research
- EU
- Netherlands Proteomics Centre (NPC)
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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 EMBO Journal (2009) 28, 1332-1340. doi: 10.1038/emboj.2009.65; Published online 19 March 2009
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