1lfw

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spinqualitylabelsall models 1lfw, resolution 1.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of pepV

Overview

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.

About this Structure

1LFW is a Single protein structure of sequence from [1] with ZN and AEP as ligands. Active as Xaa-His dipeptidase, with EC number 3.4.13.3 Full crystallographic information is available from OCA.

Reference

Crystal structure of the dinuclear zinc aminopeptidase PepV from Lactobacillus delbrueckii unravels its preference for dipeptides., Jozic D, Bourenkow G, Bartunik H, Scholze H, Dive V, Henrich B, Huber R, Bode W, Maskos K, Structure. 2002 Aug;10(8):1097-106. PMID:12176387 [[Category: ]]

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