2vpt: Difference between revisions

Revision as of 19:04, 28 July 2008

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File:2vpt.png

Template:STRUCTURE 2vpt

CLOSTRIDIUM THERMOCELLUM FAMILY 3 CARBOHYDRATE ESTERASECLOSTRIDIUM THERMOCELLUM FAMILY 3 CARBOHYDRATE ESTERASE

Template:ABSTRACT PUBMED 18436237

About this StructureAbout this Structure

2VPT is a Single protein structure of sequence from Clostridium thermocellum. Full crystallographic information is available from OCA.

ReferenceReference

Crystal Structure of a Cellulosomal Family 3 Carbohydrate Esterase from Clostridium thermocellum Provides Insights into the Mechanism of Substrate Recognition., Correia MA, Prates JA, Bras J, Fontes CM, Newman JA, Lewis RJ, Gilbert HJ, Flint JE, J Mol Biol. 2008 Mar 28;. PMID:18436237

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OCA

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-'''CLOSTRIDIUM THERMOCELLUM FAMILY 3 CARBOHYDRATE ESTERASE'''
+===CLOSTRIDIUM THERMOCELLUM FAMILY 3 CARBOHYDRATE ESTERASE===
-==Overview==
+<!--
-The microbial degradation of the plant cell wall is of increasing industrial significance, exemplified by the interest in generating biofuels from plant cell walls. The majority of plant cell-wall polysaccharides are acetylated, and removal of the acetyl groups through the action of carbohydrate esterases greatly increases the efficiency of polysaccharide saccharification. Enzymes in carbohydrate esterase family 3 (CE3) are common in plant cell wall-degrading microorganisms but there is a paucity of structural and biochemical information on these biocatalysts. Clostridium thermocellum contains a single CE3 enzyme, CtCes3, which comprises two highly homologous (97% sequence identity) catalytic modules appended to a C-terminal type I dockerin that targets the esterase into the cellulosome, a large protein complex that catalyses plant cell wall degradation. Here, we report the crystal structure and biochemical properties of the N-terminal catalytic module (CtCes3-1) of CtCes3. The enzyme is a thermostable acetyl-specific esterase that exhibits a strong preference for acetylated xylan. CtCes3-1 displays an alpha/beta hydrolase fold that contains a central five-stranded parallel twisted beta-sheet flanked by six alpha-helices. In addition, the enzyme contains a canonical catalytic triad in which Ser44 is the nucleophile, His208 is the acid-base and Asp205 modulates the basic nature of the histidine. The acetate moiety is accommodated in a hydrophobic pocket and the negative charge of the tetrahedral transition state is stabilized through hydrogen bonds with the backbone N of Ser44 and Gly95 and the side-chain amide of Asn124.
+The line below this paragraph, {{ABSTRACT_PUBMED_18436237}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18436237 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_18436237}}
 ==About this Structure==
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 [[Category: Esterase]]
 [[Category: Hydrolase]]
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