2V3Y

His361Ala Escherichia coli aminopeptidase P in complex with product

2V3Y の概要

• エントリーDOI: 10.2210/pdb2v3y/pdb
• 関連するPDBエントリー: 1A16 1JAW 1M35 1N51 1W2M 1W7V 1WBQ 1WL6 1WL9 1WLR 2BH3 2BHA 2BHB 2BHC 2BHD 2BN7 2BWS 2BWT 2BWU 2BWV 2BWW 2BWX 2BWY 2V3X 2V3Z
• 分子名称: XAA-PRO AMINOPEPTIDASE, TRIPEPTIDE (VALINE-PROLINE-LEUCINE), MANGANESE (II) ION, ... (5 entities in total)
• 機能のキーワード: 'pita-bread' enzyme, proline- specific enzyme, aminopeptidase p, manganese enzyme, protease, manganese, hydrolase, metal-binding, metalloenzyme, aminopeptidase, metalloprotease
• 由来する生物種: ESCHERICHIA COLI; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 50165.74

構造登録者

Graham, S.C.,Guss, J.M. (登録日: 2007-06-25, 公開日: 2007-11-20, 最終更新日: 2024-10-23)

主引用文献

Graham, S.C.,Guss, J.M.
Complexes of Mutants of Escherichia Coli Aminopeptidase P and the Tripeptide Substrate Valproleu.
Arch.Biochem.Biophys., 469:200-208, 2008

PubMed Abstract: Aminopeptidase P (APPro) is a manganese-containing enzyme that catalyses the hydrolysis of the N-terminal residue of a polypeptide if the second residue is proline. Structures of APPro mutants with reduced or negligible activity have been determined in complex with the tripeptide substrate ValProLeu. In the complex of Glu383Ala APPro with ValProLeu one of the two metal sites is only partly occupied, indicating an essential role for Glu383 in metal binding in the presence of substrate. His361Ala APPro clearly possesses residual activity as the ValProLeu substrate has been cleaved in the crystals; difference electron density consistent with bound ProLeu dipeptide and a disordered Val amino acid is present at the active site. Contrary to previous suggestions, the His243Ala mutant is capable of binding substrate. The structure of the His243Ala APPro complex with ValProLeu shows that the peptide interacts with one of the active-site metal atoms via its terminal amino group. The implications of these complexes for the roles of the respective residues in APPro catalysis are discussed.

PubMed: 17983589
DOI: 10.1016/J.ABB.2007.10.009

実験手法

X-RAY DIFFRACTION (1.6 Å)