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[[Image:1daq.gif|left|200px]]
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[[Image:1daq.png|left|200px]]


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{{STRUCTURE_1daq|  PDB=1daq  |  SCENE=  }}  
{{STRUCTURE_1daq|  PDB=1daq  |  SCENE=  }}  


'''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)===




==Overview==
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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.
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==About this Structure==
==About this Structure==
1DAQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DAQ OCA].  
1DAQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DAQ OCA].  


==Reference==
==Reference==
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[[Category: Cellulose degradation]]
[[Category: Cellulose degradation]]
[[Category: Cellulosome]]
[[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 Mon Jun 30 22:45:18 2008''

Revision as of 19:45, 30 June 2008

File:1daq.png

Template:STRUCTURE 1daq

SOLUTION STRUCTURE OF THE TYPE I DOCKERIN DOMAIN FROM THE CLOSTRIDIUM THERMOCELLUM CELLULOSOME (MINIMIZED AVERAGE STRUCTURE)

Template:ABSTRACT PUBMED 11273698

About this Structure

1DAQ is a Single protein structure of sequence from Clostridium thermocellum. Full experimental 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 Mon Jun 30 22:45:18 2008

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