1lfw | pdb_00001lfw
Crystal structure of pepV
Structural highlights
Function[PEPV_LACDL] Is a relatively unspecific dipeptidase cleaving a variety of dipeptides, notably those with an N-terminal beta-Ala or D-Ala residue, e.g. carnosine (beta-Ala-His). To a lesser extent, also shows aminopeptidase activity, since it is able to catalyze the removal of the N-terminal amino acid from a few distinct tripeptides.[1] 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 PubMedPepV 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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