1ju4: Difference between revisions

Revision as of 20:52, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ju4.png

Template:STRUCTURE 1ju4

BACTERIAL COCAINE ESTERASE COMPLEX WITH PRODUCTBACTERIAL COCAINE ESTERASE COMPLEX WITH PRODUCT

Template:ABSTRACT PUBMED 11742345

About this StructureAbout this Structure

1JU4 is a Single protein structure of sequence from Rhodococcus sp. mb1. Full crystallographic information is available from OCA.

ReferenceReference

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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-'''BACTERIAL COCAINE ESTERASE COMPLEX WITH PRODUCT'''
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-==Overview==
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-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.
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 [[Category: Wilson, I A.]]
 [[Category: Alpha/beta hydrolase]]
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