1usw
From Proteopedia
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CRYSTAL STRUCTURE OF FERULIC ACID ESTERASE FROM ASPERGILLUS NIGER
Overview
As a component of the array of enzymes produced by micro-organisms to, deconstruct plant cell walls, feruloyl esterases hydrolyze phenolic groups, involved in the cross-linking of arabinoxylan to other polymeric, structures. This is important for opening the cell wall structure, making, material more accessible to glycosyl hydrolases. Here, we describe the, first crystal structure of the non-modular type-A feruloyl esterase from, Aspergillus niger (AnFaeA) solved at 2.5A resolution. AnFaeA displays an, alpha/beta hydrolase fold similar to that found in fungal lipases and, different from that reported for other feruloyl esterases., Crystallographic and site-directed mutagenesis studies allow us to, identify the catalytic triad (Ser133-His247-Asp194) that forms the, catalytic machinery of ... [(full description)]
About this Structure
1USW is a [Single protein] structure of sequence from [Aspergillus niger] with SO4 as [ligand]. Active as [Feruloyl esterase], with EC number [3.1.1.73]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
The crystal structure of feruloyl esterase A from Aspergillus niger suggests evolutive functional convergence in feruloyl esterase family., Hermoso JA, Sanz-Aparicio J, Molina R, Juge N, Gonzalez R, Faulds CB, J Mol Biol. 2004 Apr 30;338(3):495-506. PMID:15081808
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