This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1lam
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1lam.jpg|left|200px]] | + | [[Image:1lam.jpg|left|200px]] |
| - | + | ||
| - | '''LEUCINE AMINOPEPTIDASE (UNLIGATED)''' | + | {{Structure |
| + | |PDB= 1lam |SIZE=350|CAPTION= <scene name='initialview01'>1lam</scene>, resolution 1.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</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 (UNLIGATED)''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1LAM is a [ | + | 1LAM 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=1LAM 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]] | ||
| Line 23: | Line 32: | ||
[[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 12:28:37 2008'' |
Revision as of 10:28, 20 March 2008
| |||||||
| , resolution 1.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Activity: | Leucyl aminopeptidase, with EC number 3.4.11.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
LEUCINE AMINOPEPTIDASE (UNLIGATED)
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
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
Page seeded by OCA on Thu Mar 20 12:28:37 2008
