1LFW

Crystal structure of pepV

1LFW の概要

• エントリーDOI: 10.2210/pdb1lfw/pdb
• 分子名称: pepV, ZINC ION, 3-[(1-AMINO-2-CARBOXY-ETHYL)-HYDROXY-PHOSPHINOYL]-2-METHYL-PROPIONIC ACID, ... (4 entities in total)
• 機能のキーワード: hydrolase, dipeptidase
• 由来する生物種: Lactobacillus delbrueckii
• 細胞内の位置: Cytoplasm (Probable): P45494
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52415.09

構造登録者

Jozic, D.,Bourenkow, G.,Bartunik, H.,Scholze, H.,Dive, V.,Henrich, B.,Huber, R.,Bode, W.,Maskos, K. (登録日: 2002-04-12, 公開日: 2002-10-23, 最終更新日: 2024-03-13)

主引用文献

Jozic, D.,Bourenkow, G.,Bartunik, H.,Scholze, H.,Dive, V.,Henrich, B.,Huber, R.,Bode, W.,Maskos, K.
Crystal Structure of the Dinuclear Zinc Aminopeptidase PepV from Lactobacillus delbrueckii Unravels Its Preference for Dipeptides
Structure, 10:1097-1106, 2002

PubMed Abstract: PepV from Lactobacillus delbrueckii, a dinuclear zinc peptidase, has been characterized as an unspecific amino dipeptidase. The crystal structure of PepV in complex with the phosphinic inhibitor AspPsi[PO(2)CH(2)]AlaOH, a dipeptide substrate mimetic, reveals a "catalytic domain" and a "lid domain," which together form an internal active site cavity that traps the inhibitor. The catalytic domain is topologically similar to catalytic domains from amino- and carboxypeptidases. However, the lid domain is unique among the related enzymes. In contrast to the other related exopeptidases, PepV recognizes and fixes the dipeptide backbone, while the side chains are not specifically probed and can vary, rendering it a nonspecific dipeptidase. The cocrystallized inhibitor illustrates the two roles of the two catalytic zinc ions, namely stabilization of the tetrahedral intermediate and activation of the catalytic water molecule.

PubMed: 12176387
DOI: 10.1016/S0969-2126(02)00805-5

実験手法

X-RAY DIFFRACTION (1.8 Å)