2c79

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spinqualitylabelsall models 2c79, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

THE STRUCTURE OF A FAMILY 4 ACETYL XYLAN ESTERASE FROM CLOSTRIDIUM THERMOCELLUM IN COMPLEX WITH A COLBALT ION.

Overview

The enzymatic degradation of plant cell wall xylan requires the concerted, action of a diverse enzymatic syndicate. Among these enzymes are xylan, esterases, which hydrolyze the O-acetyl substituents, primarily at the O-2, position of the xylan backbone. All acetylxylan esterase structures, described previously display a alpha/beta hydrolase fold with a, "Ser-His-Asp" catalytic triad. Here we report the structures of two, distinct acetylxylan esterases, those from Streptomyces lividans and, Clostridium thermocellum, in native and complex forms, with x-ray data to, between 1.6 and 1.0 A resolution. We show, using a novel linked assay, system with PNP-2-O-acetylxyloside and a beta-xylosidase, that the enzymes, are sugar-specific and metal ion-dependent and possess a single metal, center ... [(full description)]

About this Structure

2C79 is a [Single protein] structure of sequence from [Clostridium thermocellum] with CO as [ligand]. Active as [Hydrolase], with EC number [3.1.1.72]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Structure and activity of two metal ion-dependent acetylxylan esterases involved in plant cell wall degradation reveals a close similarity to peptidoglycan deacetylases., Taylor EJ, Gloster TM, Turkenburg JP, Vincent F, Brzozowski AM, Dupont C, Shareck F, Centeno MS, Prates JA, Puchart V, Ferreira LM, Fontes CM, Biely P, Davies GJ, J Biol Chem. 2006 Apr 21;281(16):10968-75. Epub 2006 Jan 23. PMID:16431911

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