1daq
From Proteopedia
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'''SOLUTION STRUCTURE OF THE TYPE I DOCKERIN DOMAIN FROM THE CLOSTRIDIUM THERMOCELLUM CELLULOSOME (MINIMIZED AVERAGE STRUCTURE)''' | '''SOLUTION STRUCTURE OF THE TYPE I DOCKERIN DOMAIN FROM THE CLOSTRIDIUM THERMOCELLUM CELLULOSOME (MINIMIZED AVERAGE STRUCTURE)''' | ||
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[[Category: Westler, W M.]] | [[Category: Westler, W M.]] | ||
[[Category: Wu, J H.D.]] | [[Category: Wu, J H.D.]] | ||
| - | [[Category: | + | [[Category: Calcium-binding]] |
| - | [[Category: | + | [[Category: Cellulose degradation]] |
| - | [[Category: | + | [[Category: Cellulosome]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:38:14 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 10:38, 2 May 2008
SOLUTION STRUCTURE OF THE TYPE I DOCKERIN DOMAIN FROM THE CLOSTRIDIUM THERMOCELLUM CELLULOSOME (MINIMIZED AVERAGE STRUCTURE)
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
1DAQ is a Single protein structure of sequence from Clostridium thermocellum. 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 Page seeded by OCA on Fri May 2 13:38:14 2008
