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| {{STRUCTURE_1lan| PDB=1lan | SCENE= }} | | {{STRUCTURE_1lan| PDB=1lan | SCENE= }} |
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| '''LEUCINE AMINOPEPTIDASE COMPLEX WITH L-LEUCINAL'''
| | ===LEUCINE AMINOPEPTIDASE COMPLEX WITH L-LEUCINAL=== |
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| ==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. | | 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}} |
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| ==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 23:43:45 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 12:07:42 2008'' |