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1ukc

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(New page: 200px<br /><applet load="1ukc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ukc, resolution 2.10&Aring;" /> '''Crystal Structure of...)
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Revision as of 02:00, 25 November 2007

Image:1ukc.jpg

1ukc, resolution 2.10Å

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Crystal Structure of Aspergillus niger EstA

Overview

From the fungus Aspergillus niger, we identified a new gene encoding, protein EstA, a member of the alpha/beta-hydrolase fold superfamily but of, unknown substrate specificity. EstA was overexpressed and its crystal, structure was solved by molecular replacement using a, lipase-acetylcholinesterase chimera template. The 2.1 A resolution, structure of EstA reveals a canonical Ser/Glu/His catalytic triad located, in a small pocket at the bottom of a large solvent-accessible, bowl-shaped, cavity. Potential substrates selected by manual docking procedures were, assayed for EstA activity. Consistent with the pocket geometry, preference, for hydrolysis of short acyl/propyl chain substrates was found., Identification of close homologs from the genome of other fungi, of which, some are broad host-range pathogens, defines EstA as the first member of a, novel class of fungal esterases within the superfamily. Hence the, structure of EstA constitutes a lead template in the design of new, antifungal agents directed toward its pathogenic homologs.

About this Structure

1UKC is a Single protein structure of sequence from Aspergillus niger with NAG, MAN, SO4, CL and EDO as ligands. Full crystallographic information is available from OCA.

Reference

Aspergillus niger protein EstA defines a new class of fungal esterases within the alpha/beta hydrolase fold superfamily of proteins., Bourne Y, Hasper AA, Chahinian H, Juin M, De Graaff LH, Marchot P, Structure. 2004 Apr;12(4):677-87. PMID:15062090

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