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| - | [[Image:1edg.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1edg| PDB=1edg | SCENE= }} | | {{STRUCTURE_1edg| PDB=1edg | SCENE= }} |
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| - | '''SINGLE CRYSTAL STRUCTURE DETERMINATION OF THE CATALYTIC DOMAIN OF CELCCA CARRIED OUT AT 15 DEGREE C'''
| + | ===SINGLE CRYSTAL STRUCTURE DETERMINATION OF THE CATALYTIC DOMAIN OF CELCCA CARRIED OUT AT 15 DEGREE C=== |
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| - | ==Overview==
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| - | BACKGROUND: Cellulases are glycosyl hydrolases--enzymes that hydrolyze glycosidic bonds. They have been widely studied using biochemical and microbiological techniques and have attracted industrial interest because of their potential in biomass conversion and in the paper and textile industries. Glycosyl hydrolases have lately been assigned to specific families on the basis of similarities in their amino acid sequences. The cellulase endoglucanase A produced by Clostridium cellulolyticum (CelCCA) belongs to family 5. RESULTS: We have determined the crystal structure of the catalytic domain of CelCCA at a resolution of 2.4 A and refined it to 1.6 A. The structure was solved by the multiple isomorphous replacement method. The overall structural fold, (alpha/beta)8, belongs to the TIM barrel motif superfamily. The catalytic centre is located at the C-terminal ends of the beta strands; the aromatic residues, forming the substrate-binding site, are arranged along a long cleft on the surface of the globular enzyme. CONCLUSIONS: Strictly conserved residues within family 5 are described with respect to their catalytic function. The proton donor, Glu170, and the nucleophile, Glu307, are localized on beta strands IV and VII, respectively, and are separated by 5.5 A, as expected for enzymes which retain the configuration of the substrate's anomeric carbon. Structure determination of the catalytic domain of CelCCA allows a comparison with related enzymes belonging to glycosyl hydrolase families 2, 10 and 17, which also display an (alpha/beta)8 fold.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8535787}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8535787 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8535787}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Family some]] | | [[Category: Family some]] |
| | [[Category: Xylanase]] | | [[Category: Xylanase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:57:41 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:31:47 2008'' |
Revision as of 21:31, 30 June 2008
Template:STRUCTURE 1edg
SINGLE CRYSTAL STRUCTURE DETERMINATION OF THE CATALYTIC DOMAIN OF CELCCA CARRIED OUT AT 15 DEGREE C
Template:ABSTRACT PUBMED 8535787
About this Structure
1EDG is a Single protein structure of sequence from Clostridium cellulolyticum. Full crystallographic information is available from OCA.
Reference
Crystal structure of the catalytic domain of a bacterial cellulase belonging to family 5., Ducros V, Czjzek M, Belaich A, Gaudin C, Fierobe HP, Belaich JP, Davies GJ, Haser R, Structure. 1995 Sep 15;3(9):939-49. PMID:8535787
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