1dpp
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DIPEPTIDE BINDING PROTEIN COMPLEX WITH GLYCYL-L-LEUCINE
OverviewOverview
The Escherichia coli periplasmic dipeptide binding protein functions in, both peptide transport and taxis toward peptides. The structure of the, dipeptide binding protein in complex with Gly-Leu (glycyl-L-leucine) has, been determined at 3.2 A resolution. The binding site for dipeptides is, designed to recognize the ligand's backbone while providing space to, accommodate a variety of side chains. Some repositioning of protein side, chains lining the binding site must occur when the dipeptide's second, residue is larger than leucine. The protein's fold is very similar to that, of the Salmonella typhimurium oligopeptide binding protein, and a, comparison of the structures reveals the structural basis for the, dipeptide binding protein's preference for shorter peptides.
About this StructureAbout this Structure
1DPP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the dipeptide binding protein from Escherichia coli involved in active transport and chemotaxis., Dunten P, Mowbray SL, Protein Sci. 1995 Nov;4(11):2327-34. PMID:8563629
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