1lam: Difference between revisions

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[[Image:1lam.jpg|left|200px]]
{{Seed}}
[[Image:1lam.png|left|200px]]


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{{STRUCTURE_1lam|  PDB=1lam  |  SCENE=  }}  
{{STRUCTURE_1lam|  PDB=1lam  |  SCENE=  }}  


'''LEUCINE AMINOPEPTIDASE (UNLIGATED)'''
===LEUCINE AMINOPEPTIDASE (UNLIGATED)===




==Overview==
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The three-dimensional structures of bovine lens leucine aminopeptidase (blLAP) complexed with L-leucinal and of the unliganded enzyme have been determined at crystallographic resolutions of 1.9 and 1.6 A, respectively. Leucinal binds as a hydrated gem-diol to the active site of b1LAP), resembling the presumed gem-diolated intermediate in the catalytic pathway. One hydroxyl group bridges the two active site metal ions, and the other OH group is coordinated to Zn1. The high-resolution structure of the unliganded enzyme reveals one metal-bound water ligand, which is bridging both zinc ions. Together, these structures support a mechanism in which the bridging water ligand is the attacking hydroxide ion nucleophile. The gem-diolate intermediate is probably stabilized by four coordinating bonds to the dizinc center and by interaction with Lys-262 and Arg-336. In the mechanism, Lys-262 polarizes the peptide carbonyl group, which is also coordinated to Zn1. The Arg-336 side chain interacts with the substrate and the gem-diolate intermediate via water molecules. Near Arg-336 in the b1LAP-leucinal structure, an unusually short hydrogen bond is found between two active site water molecules.
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{{ABSTRACT_PUBMED_7578088}}


==About this Structure==
==About this Structure==
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[[Category: Exopeptidase]]
[[Category: Exopeptidase]]
[[Category: Metallopeptidase]]
[[Category: Metallopeptidase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:43:40 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 12:07:41 2008''

Revision as of 09:07, 2 July 2008

File:1lam.png

Template:STRUCTURE 1lam

LEUCINE AMINOPEPTIDASE (UNLIGATED)

Template:ABSTRACT PUBMED 7578088

About this Structure

1LAM is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Two-metal ion mechanism of bovine lens leucine aminopeptidase: active site solvent structure and binding mode of L-leucinal, a gem-diolate transition state analogue, by X-ray crystallography., Strater N, Lipscomb WN, Biochemistry. 1995 Nov 14;34(45):14792-800. PMID:7578088

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