1l2a
From Proteopedia
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| - | [[Image:1l2a.jpg|left|200px]] | + | [[Image:1l2a.jpg|left|200px]] |
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| - | '''The Crystal Structure and Catalytic Mechanism of Cellobiohydrolase CelS, the Major Enzymatic Component of the Clostridium thermocellum cellulosome''' | + | {{Structure |
| + | |PDB= 1l2a |SIZE=350|CAPTION= <scene name='initialview01'>1l2a</scene>, resolution 2.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |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= cels ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1515 Clostridium thermocellum]) | ||
| + | }} | ||
| + | |||
| + | '''The Crystal Structure and Catalytic Mechanism of Cellobiohydrolase CelS, the Major Enzymatic Component of the Clostridium thermocellum cellulosome''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1L2A is a [ | + | 1L2A 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=1L2A OCA]. |
==Reference== | ==Reference== | ||
| - | The crystal structure and catalytic mechanism of cellobiohydrolase CelS, the major enzymatic component of the Clostridium thermocellum Cellulosome., Guimaraes BG, Souchon H, Lytle BL, David Wu JH, Alzari PM, J Mol Biol. 2002 Jul 12;320(3):587-96. PMID:[http:// | + | The crystal structure and catalytic mechanism of cellobiohydrolase CelS, the major enzymatic component of the Clostridium thermocellum Cellulosome., Guimaraes BG, Souchon H, Lytle BL, David Wu JH, Alzari PM, J Mol Biol. 2002 Jul 12;320(3):587-96. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12096911 12096911] |
[[Category: Cellulase]] | [[Category: Cellulase]] | ||
[[Category: Clostridium thermocellum]] | [[Category: Clostridium thermocellum]] | ||
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[[Category: alpha/alpha barrel]] | [[Category: alpha/alpha barrel]] | ||
| - | ''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 12:25:20 2008'' |
Revision as of 10:25, 20 March 2008
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| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | cels (Clostridium thermocellum) | ||||||
| Activity: | Cellulase, with EC number 3.2.1.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The Crystal Structure and Catalytic Mechanism of Cellobiohydrolase CelS, the Major Enzymatic Component of the Clostridium thermocellum cellulosome
Overview
Cellobiohydrolase CelS plays an important role in the cellulosome, an active cellulase system produced by the thermophilic anaerobe Clostridium thermocellum. The structures of the catalytic domain of CelS in complex with substrate (cellohexaose) and product (cellobiose) were determined at 2.5 and 2.4 A resolution, respectively. The protein folds into an (alpha/alpha)(6) barrel with a tunnel-shaped substrate-binding region. The conformation of the loops defining the tunnel is intrinsically stable in the absence of substrate, suggesting a model to account for the processive mode of action of family 48 cellobiohydrolases. Structural comparisons with other (alpha/alpha)(6) barrel glycosidases indicate that CelS and endoglucanase CelA, a sequence-unrelated family 8 glycosidase with a groove-shaped substrate-binding region, use the same catalytic machinery to hydrolyze the glycosidic linkage, despite a low sequence similarity and a different endo/exo mode of action. A remarkable feature of the mechanism is the absence, from CelS, of a carboxylic group acting as the base catalyst. The nearly identical arrangement of substrate and functionally important residues in the two active sites strongly suggests an evolutionary relationship between the cellobiohydrolase and endoglucanase families, which can therefore be classified into a new clan of glycoside hydrolases.
About this Structure
1L2A is a Single protein structure of sequence from Clostridium thermocellum. Full crystallographic information is available from OCA.
Reference
The crystal structure and catalytic mechanism of cellobiohydrolase CelS, the major enzymatic component of the Clostridium thermocellum Cellulosome., Guimaraes BG, Souchon H, Lytle BL, David Wu JH, Alzari PM, J Mol Biol. 2002 Jul 12;320(3):587-96. PMID:12096911
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