1DPP
DIPEPTIDE BINDING PROTEIN COMPLEX WITH GLYCYL-L-LEUCINE
1DPP の概要
| エントリーDOI | 10.2210/pdb1dpp/pdb |
| 分子名称 | DIPEPTIDE BINDING PROTEIN, GLYCINE, LEUCINE (3 entities in total) |
| 機能のキーワード | chemotaxis, complex (binding protein-peptide) complex, peptide binding protein |
| 由来する生物種 | Escherichia coli |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 230728.41 |
| 構造登録者 | |
| 主引用文献 | Dunten, P.,Mowbray, S.L. Crystal structure of the dipeptide binding protein from Escherichia coli involved in active transport and chemotaxis. Protein Sci., 4:2327-2334, 1995 Cited by PubMed Abstract: 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. PubMed: 8563629主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.2 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






