1daq
From Proteopedia
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|PDB= 1daq |SIZE=350|CAPTION= <scene name='initialview01'>1daq</scene> | |PDB= 1daq |SIZE=350|CAPTION= <scene name='initialview01'>1daq</scene> | ||
|SITE= <scene name='pdbsite=I:First+Predicted+Ca2++Binding+Loop'>I</scene> and <scene name='pdbsite=II:Second+Predicted+Ca2++Binding+Loop'>II</scene> | |SITE= <scene name='pdbsite=I:First+Predicted+Ca2++Binding+Loop'>I</scene> and <scene name='pdbsite=II:Second+Predicted+Ca2++Binding+Loop'>II</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1dav|1DAV]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1daq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1daq OCA], [http://www.ebi.ac.uk/pdbsum/1daq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1daq RCSB]</span> | ||
}} | }} | ||
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[[Category: Westler, W M.]] | [[Category: Westler, W M.]] | ||
[[Category: Wu, J H.D.]] | [[Category: Wu, J H.D.]] | ||
| - | [[Category: CA]] | ||
[[Category: calcium-binding]] | [[Category: calcium-binding]] | ||
[[Category: cellulose degradation]] | [[Category: cellulose degradation]] | ||
[[Category: cellulosome]] | [[Category: cellulosome]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:38:03 2008'' |
Revision as of 16:38, 30 March 2008
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| Sites: | and | ||||||
| Ligands: | |||||||
| Activity: | Cellulase, with EC number 3.2.1.4 | ||||||
| Related: | 1DAV
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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