1ju3
From Proteopedia
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|PDB= 1ju3 |SIZE=350|CAPTION= <scene name='initialview01'>1ju3</scene>, resolution 1.58Å | |PDB= 1ju3 |SIZE=350|CAPTION= <scene name='initialview01'>1ju3</scene>, resolution 1.58Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PBC:PHENYL BORONIC ACID'>PBC</scene> | + | |LIGAND= <scene name='pdbligand=PBC:PHENYL+BORONIC+ACID'>PBC</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ju4|1JU4]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ju3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ju3 OCA], [http://www.ebi.ac.uk/pdbsum/1ju3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ju3 RCSB]</span> | ||
}} | }} | ||
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[[Category: Turner, J M.]] | [[Category: Turner, J M.]] | ||
[[Category: Wilson, I A.]] | [[Category: Wilson, I A.]] | ||
| - | [[Category: PBC]] | ||
[[Category: alpha/beta hydrolase]] | [[Category: alpha/beta hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:38:58 2008'' |
Revision as of 18:39, 30 March 2008
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| , resolution 1.58Å | |||||||
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| Ligands: | |||||||
| Related: | 1JU4
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BACTERIAL COCAINE ESTERASE COMPLEX WITH TRANSITION STATE ANALOG
Overview
Here we report the first structure of a cocaine-degrading enzyme. The bacterial esterase, cocE, hydrolyzes pharmacologically active (-)-cocaine to a non-psychoactive metabolite with a rate faster than any other reported cocaine esterase (kcat = 7.8 s-1 and KM = 640 nM). Because of the high catalytic proficiency of cocE, it is an attractive candidate for novel protein-based therapies for cocaine overdose. The crystal structure of cocE, solved by multiple anomalous dispersion (MAD) methods, reveals that cocE is a serine esterase composed of three domains: (i) a canonical alpha/beta hydrolase fold (ii) an alpha-helical domain that caps the active site and (iii) a jelly-roll-like beta-domain that interacts extensively with the other two domains. The active site was identified within the interface of all three domains by analysis of the crystal structures of transition state analog adduct and product complexes, which were refined at 1.58 A and 1.63 A resolution, respectively. These structural studies suggest that substrate recognition arises partly from interactions between the benzoyl moiety of cocaine and a highly evolved specificity pocket.
About this Structure
1JU3 is a Single protein structure of sequence from Rhodococcus sp. mb1. Full crystallographic information is available from OCA.
Reference
Crystal structure of a bacterial cocaine esterase., Larsen NA, Turner JM, Stevens J, Rosser SJ, Basran A, Lerner RA, Bruce NC, Wilson IA, Nat Struct Biol. 2002 Jan;9(1):17-21. PMID:11742345
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