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1uza

From Proteopedia

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{{STRUCTURE_1uza| PDB=1uza | SCENE= }}
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'''CRYSTALLOGRAPHIC STRUCTURE OF A FERULOYL ESTERASE FROM ASPERGILLUS NIGER'''
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===CRYSTALLOGRAPHIC STRUCTURE OF A FERULOYL ESTERASE FROM ASPERGILLUS NIGER===
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==Overview==
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The crystallographic structure of feruloyl esterase from Aspergillus niger has been determined to a resolution of 1.5 A by molecular replacement. The protein has an alpha/beta-hydrolase structure with a Ser-His-Asp catalytic triad; the overall fold of the protein is very similar to that of the fungal lipases. The structure of the enzyme-product complex was determined to a resolution of 1.08 A and reveals dual conformations for the serine and histidine residues at the active site.
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{{ABSTRACT_PUBMED_15103133}}
==About this Structure==
==About this Structure==
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[[Category: Serine esterase]]
[[Category: Serine esterase]]
[[Category: Xylan degradation]]
[[Category: Xylan degradation]]
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Revision as of 09:18, 29 July 2008

Image:1uza.png

Template:STRUCTURE 1uza

CRYSTALLOGRAPHIC STRUCTURE OF A FERULOYL ESTERASE FROM ASPERGILLUS NIGER

Template:ABSTRACT PUBMED 15103133

About this Structure

1UZA is a Single protein structure of sequence from Aspergillus niger. Full crystallographic information is available from OCA.

Reference

Structure of a feruloyl esterase from Aspergillus niger., McAuley KE, Svendsen A, Patkar SA, Wilson KS, Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):878-87. Epub 2004, Apr 21. PMID:15103133

Page seeded by OCA on Tue Jul 29 12:18:03 2008

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