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'''LEUCINE AMINOPEPTIDASE COMPLEX WITH L-LEUCINAL''' | '''LEUCINE AMINOPEPTIDASE COMPLEX WITH L-LEUCINAL''' | ||
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[[Category: Lipscomb, W N.]] | [[Category: Lipscomb, W N.]] | ||
[[Category: Straeter, N.]] | [[Category: Straeter, N.]] | ||
[[Category: | [[Category: Aminopeptidase]] | ||
[[Category: | [[Category: Exopeptidase]] | ||
[[Category: | [[Category: Metallopeptidase]] | ||
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Revision as of 23:43, 2 May 2008
LEUCINE AMINOPEPTIDASE COMPLEX WITH L-LEUCINAL
OverviewOverview
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.
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 Fri May 2 23:43:45 2008