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1lan
From Proteopedia
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| - | [[Image:1lan.gif|left|200px]] | + | [[Image:1lan.gif|left|200px]] |
| - | + | ||
| - | '''LEUCINE AMINOPEPTIDASE COMPLEX WITH L-LEUCINAL''' | + | {{Structure |
| + | |PDB= 1lan |SIZE=350|CAPTION= <scene name='initialview01'>1lan</scene>, resolution 1.9Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=LEU:LEUCINE'>LEU</scene> and <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Leucyl_aminopeptidase Leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.1 3.4.11.1] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''LEUCINE AMINOPEPTIDASE COMPLEX WITH L-LEUCINAL''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LAN is a [ | + | 1LAN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAN OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7578088 7578088] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Leucyl aminopeptidase]] | [[Category: Leucyl aminopeptidase]] | ||
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[[Category: metallopeptidase]] | [[Category: metallopeptidase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:28:36 2008'' |
Revision as of 10:28, 20 March 2008
| |||||||
| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Activity: | Leucyl aminopeptidase, with EC number 3.4.11.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
About this Structure
1LAN 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
Page seeded by OCA on Thu Mar 20 12:28:36 2008
