1ukc

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{{STRUCTURE_1ukc| PDB=1ukc | SCENE= }}
{{STRUCTURE_1ukc| PDB=1ukc | SCENE= }}
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'''Crystal Structure of Aspergillus niger EstA'''
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===Crystal Structure of Aspergillus niger EstA===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15062090 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15062090}}
==About this Structure==
==About this Structure==
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[[Category: Esterase]]
[[Category: Esterase]]
[[Category: Fungi]]
[[Category: Fungi]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:20:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:18:39 2008''

Revision as of 17:18, 27 July 2008

Image:1ukc.png

Template:STRUCTURE 1ukc

Crystal Structure of Aspergillus niger EstA

Template:ABSTRACT PUBMED 15062090

About this Structure

1UKC is a Single protein structure of sequence from Aspergillus niger. 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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