1lfw
From Proteopedia
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[[Image:1lfw.gif|left|200px]] | [[Image:1lfw.gif|left|200px]] | ||
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| - | | | + | {{STRUCTURE_1lfw| PDB=1lfw | SCENE= }} |
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'''Crystal structure of pepV''' | '''Crystal structure of pepV''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LFW is a [[Single protein]] structure | + | 1LFW is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LFW OCA]. |
==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/12176387 12176387] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12176387 12176387] | ||
| - | [[Category: ]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Xaa-His dipeptidase]] | [[Category: Xaa-His dipeptidase]] | ||
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[[Category: Maskos, K.]] | [[Category: Maskos, K.]] | ||
[[Category: Scholze, H.]] | [[Category: Scholze, H.]] | ||
| - | [[Category: | + | [[Category: Dipeptidase]] |
| - | [[Category: | + | [[Category: Hydrolase]] |
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 20:53, 2 May 2008
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. 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 Page seeded by OCA on Fri May 2 23:53:00 2008
