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| - | [[Image:1g1k.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1g1k| PDB=1g1k | SCENE= }} | | {{STRUCTURE_1g1k| PDB=1g1k | SCENE= }} |
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| - | '''COHESIN MODULE FROM THE CELLULOSOME OF CLOSTRIDIUM CELLULOLYTICUM'''
| + | ===COHESIN MODULE FROM THE CELLULOSOME OF CLOSTRIDIUM CELLULOLYTICUM=== |
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| - | ==Overview==
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| - | In the assembly of the Clostridium cellulolyticum cellulosome, the multiple cohesin modules of the scaffolding protein CipC serve as receptors for cellulolytic enzymes which bear a dockerin module. The X-ray structure of a type I C. cellulolyticum cohesin module (Cc-cohesin) has been solved using molecular replacement, and refined at 2.0 A resolution. Despite a rather low sequence identity of 32 %, this module has a fold close to those of the two Clostridium thermocellum cohesin (Ct-cohesin) modules whose 3D structures have been determined previously. Cc-cohesin forms a dimer in the crystal, as do the two Ct-cohesins. We show here that the dimer exists in solution and that addition of dockerin-containing proteins dissociates the dimer. This suggests that the dimerization interface and the cohesin/dockerin interface may overlap. The nature of the overall surface and of the dimer interface of Cc-cohesin differ notably from those of the Ct-cohesin modules, being much less polar, and this may explain the species specificity observed in the cohesin/dockerin interaction of C. cellulolyticum and C. thermocellum. We have produced a topology model of a C. cellulolyticum dockerin and of a Cc-cohesin/dockerin complex using homology modeling and available biochemical data. Our model suggests that a special residue pair, already identified in dockerin sequences, is located at the center of the cohesin surface putatively interacting with the dockerin.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11080455}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11080455 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11080455}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Spinelli, S.]] | | [[Category: Spinelli, S.]] |
| | [[Category: Beta -barrel]] | | [[Category: Beta -barrel]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:01:09 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:16:03 2008'' |
Revision as of 01:16, 1 July 2008
Template:STRUCTURE 1g1k
COHESIN MODULE FROM THE CELLULOSOME OF CLOSTRIDIUM CELLULOLYTICUM
Template:ABSTRACT PUBMED 11080455
About this Structure
1G1K is a Single protein structure of sequence from Clostridium cellulolyticum. Full crystallographic information is available from OCA.
Reference
Crystal structure of a cohesin module from Clostridium cellulolyticum: implications for dockerin recognition., Spinelli S, Fierobe HP, Belaich A, Belaich JP, Henrissat B, Cambillau C, J Mol Biol. 2000 Nov 24;304(2):189-200. PMID:11080455
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