1dav
From Proteopedia
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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, mean structure. The structure consists of two Ca(2+)-binding loop-helix, motifs connected by a linker; the E helices entering each loop of the, classical EF-hand motif are absent from the dockerin domain. Each dockerin, Ca(2+)-binding subdomain is stabilized by a cluster of buried hydrophobic, side-chains. Structural comparisons reveal that, in its non-complexed, state, the dockerin fold displays a dramatic departure from that of, Ca(2+)-bound EF-hand domains. A putative cohesin-binding surface, comprised of conserved hydrophobic and basic residues, is proposed, providing new insight into cellulosome assembly.
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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