1h6x: Difference between revisions
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Revision as of 16:26, 30 October 2007
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THE ROLE OF CONSERVED AMONI ACIDS IN THE CLEFT OF THE C-TERMINAL FAMILY 22 CARBOHYDRATE BINDING MODULE OF CLOSTRIDIUM THERMOCELLUM XYN10B IN LIGAND BINDING
OverviewOverview
The majority of plant cell wall hydrolases are modular enzymes which, in, addition to a catalytic module, possess one or more carbohydrate-binding, modules (CBMs). These carbohydrate-active enzymes and their constituent, modules have been classified into a number of families based upon amino, acid sequence similarity. The Clostridium thermocellum xylanase, Xyn10B, contains two CBMs that belong to family 22 (CBM22). The crystal structure, of the C-terminal CBM22 (CBM22-2) was determined in a previous study, [Charnock, S. J., et al. (2000) Biochemistry 39, 5013--5021] and revealed, a surface cleft which presents several conserved residues that are, implicated in ligand binding. These amino acids have been substituted and, the structure and biochemical properties of the mutants analyzed. The ... [(full description)]
About this StructureAbout this Structure
1H6X is a [Single protein] structure of sequence from [Clostridium thermocellum] with CA as [ligand]. Structure known Active Site: XBS. Full crystallographic information is available from [OCA].
ReferenceReference
Clostridium thermocellum Xyn10B carbohydrate-binding module 22-2: the role of conserved amino acids in ligand binding., Xie H, Gilbert HJ, Charnock SJ, Davies GJ, Williamson MP, Simpson PJ, Raghothama S, Fontes CM, Dias FM, Ferreira LM, Bolam DN, Biochemistry. 2001 Aug 7;40(31):9167-76. PMID:11478884
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