1dav

From Proteopedia

Revision as of 12:56, 30 October 2007

SOLUTION STRUCTURE OF THE TYPE I DOCKERIN DOMAIN FROM THE CLOSTRIDIUM THERMOCELLUM CELLULOSOME (20 STRUCTURES)

Overview

The type I dockerin domain is responsible for incorporating its associated, glycosyl hydrolase into the bacterial cellulosome, a multienzyme, cellulolytic complex, via its interaction with a receptor domain (cohesin, domain) of the cellulosomal scaffolding subunit. The highly conserved, dockerin domain is characterized by two Ca(2+)-binding sites with sequence, similarity to the EF-hand motif. Here, we present the three-dimensional, solution structure of the 69 residue dockerin domain of Clostridium, thermocellum cellobiohydrolase CelS. Torsion angle dynamics calculations, utilizing a total of 728 NOE-derived distance constraints and 79 torsion, angle restraints yielded an ensemble of 20 structures with an average, backbone r.m.s.d. for residues 5 to 29 and 32 to 66 of 0.54 A from the, ... [(full description)]

About this Structure

1DAV is a [Single protein] structure of sequence from [Clostridium thermocellum] with CA as [ligand]. Active as [Cellulase], with EC number [3.2.1.4]. Structure known Active Sites: I and II. Full crystallographic information is available from [OCA].

Reference

Solution structure of a type I dockerin domain, a novel prokaryotic, extracellular calcium-binding domain., Lytle BL, Volkman BF, Westler WM, Heckman MP, Wu JH, J Mol Biol. 2001 Mar 30;307(3):745-53. PMID:11273698

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