English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  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., et al. (2002). Crystal structure of the dinuclear zinc aminopeptidase PepV from Lactobacillus delbrueckii unravels its preference for dipeptides. Structure, 10(8), 1097-1106.

Item is

Basic

show hide
Genre: Journal Article
Alternative Title : Structure

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Jozic, D.1, Author              
Bourenkow, G., Author
Bartunik, H.1, Author              
Scholze, H., Author
Dive, V., Author
Henrich, B., Author
Huber, R.2, Author              
Bode, W.2, 3, 4, Author              
Maskos, K.3, Author              
Affiliations:
1External Organizations, ou_persistent22              
2Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              
3Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565147              
4Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              

Content

show
hide
Free keywords: dinuclear; dipeptidase; phosphinic inhibitor; zinc- metallopeptidase; aminopeptidase; aminoacylase-1 family
 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[PO2CH2]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.

Details

show
hide
Language(s): eng - English
 Dates: 2002-08
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 41662
ISI: 000177396200008
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Structure
  Alternative Title : Structure
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 10 (8) Sequence Number: - Start / End Page: 1097 - 1106 Identifier: ISSN: 0969-2126