1dpp

From Proteopedia

DIPEPTIDE BINDING PROTEIN COMPLEX WITH GLYCYL-L-LEUCINE

Structural highlights

1dpp is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.2Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DPPA_ECOLI Dipeptide-binding protein of a transport system that can be subject to osmotic shock. DppA is also required for peptide chemotaxis.

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

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Dunten P, Mowbray SL. Crystal structure of the dipeptide binding protein from Escherichia coli involved in active transport and chemotaxis. Protein Sci. 1995 Nov;4(11):2327-34. PMID:8563629