1lan: Difference between revisions

Revision as of 12:07, 2 July 2008

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File:1lan.png

Template:STRUCTURE 1lan

LEUCINE AMINOPEPTIDASE COMPLEX WITH L-LEUCINALLEUCINE AMINOPEPTIDASE COMPLEX WITH L-LEUCINAL

Template:ABSTRACT PUBMED 7578088

About this StructureAbout this Structure

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

ReferenceReference

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

Page seeded by OCA on Wed Jul 2 12:07:42 2008

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OCA

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-[[Image:1lan.gif|left|200px]]
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 {{STRUCTURE_1lan|  PDB=1lan  |  SCENE=  }}
-'''LEUCINE AMINOPEPTIDASE COMPLEX WITH L-LEUCINAL'''
+===LEUCINE AMINOPEPTIDASE COMPLEX WITH L-LEUCINAL===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_7578088}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7578088 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_7578088}}
 ==About this Structure==
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 [[Category: Exopeptidase]]
 [[Category: Metallopeptidase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:43:45 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 12:07:42 2008''