1gmm: Difference between revisions

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[[Image:1gmm.gif|left|200px]]
{{Seed}}
[[Image:1gmm.png|left|200px]]


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{{STRUCTURE_1gmm|  PDB=1gmm  |  SCENE=  }}  
{{STRUCTURE_1gmm|  PDB=1gmm  |  SCENE=  }}  


'''CARBOHYDRATE BINDING MODULE CBM6 FROM XYLANASE U CLOSTRIDIUM THERMOCELLUM'''
===CARBOHYDRATE BINDING MODULE CBM6 FROM XYLANASE U CLOSTRIDIUM THERMOCELLUM===




==Overview==
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Polysaccharide-degrading enzymes are generally modular proteins that contain non-catalytic carbohydrate-binding modules (CBMs), which potentiate the activity of the catalytic module. CBMs have been grouped into sequence-based families, and three-dimensional structural data are available for half of these families. Clostridium thermocellum xylanase 11A is a modular enzyme that contains a CBM from family 6 (CBM6), for which no structural data are available. We have determined the crystal structure of this module to a resolution of 2.1 A. The protein is a beta-sandwich that contains two potential ligand-binding clefts designated cleft A and B. The CBM interacts primarily with xylan, and NMR spectroscopy coupled with site-directed mutagenesis identified cleft A, containing Trp-92, Tyr-34, and Asn-120, as the ligand-binding site. The overall fold of CBM6 is similar to proteins in CBM families 4 and 22, although surprisingly the ligand-binding site in CBM4 and CBM22 is equivalent to cleft B in CBM6. These structural data define a superfamily of CBMs, comprising CBM4, CBM6, and CBM22, and demonstrate that, although CBMs have evolved from a relatively small number of ancestors, the structural elements involved in ligand recognition have been assembled at different locations on the ancestral scaffold.
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{{ABSTRACT_PUBMED_11673472}}


==About this Structure==
==About this Structure==
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[[Category: Cbm family 6]]
[[Category: Cbm family 6]]
[[Category: Xylan binding]]
[[Category: Xylan binding]]
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