1dav
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1dav.gif|left|200px]]< | + | [[Image:1dav.gif|left|200px]] |
| - | + | ||
| - | '''SOLUTION STRUCTURE OF THE TYPE I DOCKERIN DOMAIN FROM THE CLOSTRIDIUM THERMOCELLUM CELLULOSOME (20 STRUCTURES)''' | + | {{Structure |
| + | |PDB= 1dav |SIZE=350|CAPTION= <scene name='initialview01'>1dav</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> | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''SOLUTION STRUCTURE OF THE TYPE I DOCKERIN DOMAIN FROM THE CLOSTRIDIUM THERMOCELLUM CELLULOSOME (20 STRUCTURES)''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1DAV is a [ | + | 1DAV 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=1DAV OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11273698 11273698] |
[[Category: Cellulase]] | [[Category: Cellulase]] | ||
[[Category: Clostridium thermocellum]] | [[Category: Clostridium thermocellum]] | ||
| Line 24: | Line 33: | ||
[[Category: cellulosome]] | [[Category: cellulosome]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:35:38 2008'' |
Revision as of 08:35, 20 March 2008
| |||||||
| Sites: | and | ||||||
| Ligands: | |||||||
| Activity: | Cellulase, with EC number 3.2.1.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Thu Mar 20 10:35:38 2008
