1lfw
From Proteopedia
(New page: 200px<br /><applet load="1lfw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lfw, resolution 1.8Å" /> '''Crystal structure of ...) |
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| - | [[Image:1lfw.gif|left|200px]]<br /><applet load="1lfw" size=" | + | [[Image:1lfw.gif|left|200px]]<br /><applet load="1lfw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lfw, resolution 1.8Å" /> | caption="1lfw, resolution 1.8Å" /> | ||
'''Crystal structure of pepV'''<br /> | '''Crystal structure of pepV'''<br /> | ||
==Overview== | ==Overview== | ||
| - | PepV from Lactobacillus delbrueckii, a dinuclear zinc peptidase, has been | + | 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== | ==About this Structure== | ||
| - | 1LFW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with ZN and AEP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Xaa-His_dipeptidase Xaa-His dipeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.13.3 3.4.13.3] Full crystallographic information is available from [http:// | + | 1LFW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=AEP:'>AEP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Xaa-His_dipeptidase Xaa-His dipeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.13.3 3.4.13.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LFW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:44:37 2008'' |
Revision as of 11:44, 21 February 2008
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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 and 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: ]]
Page seeded by OCA on Thu Feb 21 13:44:37 2008
Categories: Single protein | Xaa-His dipeptidase | Bartunik, H. | Bode, W. | Bourenkow, G. | Dive, V. | Henrich, B. | Huber, R. | Jozic, D. | Maskos, K. | Scholze, H. | AEP | ZN | Dipeptidase | Hydrolase
