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1daq
From Proteopedia
(New page: 200px<br /> <applet load="1daq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1daq" /> '''SOLUTION STRUCTURE OF THE TYPE I DOCKERIN D...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1DAQ is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum]] with CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DAQ OCA]]. | + | 1DAQ is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum]] with CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[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]]. Structure known Active Sites: I and II. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DAQ 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11273698 11273698] | 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11273698 11273698] | ||
| + | [[Category: Cellulase]] | ||
[[Category: Clostridium thermocellum]] | [[Category: Clostridium thermocellum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: cellulosome]] | [[Category: cellulosome]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:47:04 2007'' |
Revision as of 11:42, 30 October 2007
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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, ... [(full description)]
About this Structure
1DAQ 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
Page seeded by OCA on Tue Oct 30 13:47:04 2007
