1gui
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Enzymes active on complex carbohydrate polymers frequently have modular, structures in which a catalytic domain is appended to one or more, carbohydrate-binding modules (CBMs). Although CBMs have been classified, into a number of families based upon sequence, many closely related CBMs, are specific for different polysaccharides. In order to provide a, structural rationale for the recognition of different polysaccharides by, CBMs displaying a conserved fold, we have studied the thermodynamics of, binding and three-dimensional structures of the related family 4 CBMs from, Cellulomonas fimi Cel9B and Thermotoga maritima Lam16A in complex with, their ligands, beta-1,4 and beta-1,3 linked gluco-oligosaccharides, respectively. These two CBMs use a structurally conserved constellation of, ... | + | Enzymes active on complex carbohydrate polymers frequently have modular, structures in which a catalytic domain is appended to one or more, carbohydrate-binding modules (CBMs). Although CBMs have been classified, into a number of families based upon sequence, many closely related CBMs, are specific for different polysaccharides. In order to provide a, structural rationale for the recognition of different polysaccharides by, CBMs displaying a conserved fold, we have studied the thermodynamics of, binding and three-dimensional structures of the related family 4 CBMs from, Cellulomonas fimi Cel9B and Thermotoga maritima Lam16A in complex with, their ligands, beta-1,4 and beta-1,3 linked gluco-oligosaccharides, respectively. These two CBMs use a structurally conserved constellation of, aromatic and polar amino acid side-chains that interact with sugars in two, of the five binding subsites. Differences in the length and conformation, of loops in non-conserved regions create binding-site topographies that, complement the known solution conformations of their respective ligands., Thermodynamics interpreted in the light of structural information, highlights the differential role of water in the interaction of these CBMs, with their respective oligosaccharide ligands. |
==About this Structure== | ==About this Structure== | ||
| - | 1GUI is a | + | 1GUI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with BGC, CA and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GUI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: glucan]] | [[Category: glucan]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:06:33 2007'' |
Revision as of 11:01, 5 November 2007
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CBM4 STRUCTURE AND FUNCTION
Overview
Enzymes active on complex carbohydrate polymers frequently have modular, structures in which a catalytic domain is appended to one or more, carbohydrate-binding modules (CBMs). Although CBMs have been classified, into a number of families based upon sequence, many closely related CBMs, are specific for different polysaccharides. In order to provide a, structural rationale for the recognition of different polysaccharides by, CBMs displaying a conserved fold, we have studied the thermodynamics of, binding and three-dimensional structures of the related family 4 CBMs from, Cellulomonas fimi Cel9B and Thermotoga maritima Lam16A in complex with, their ligands, beta-1,4 and beta-1,3 linked gluco-oligosaccharides, respectively. These two CBMs use a structurally conserved constellation of, aromatic and polar amino acid side-chains that interact with sugars in two, of the five binding subsites. Differences in the length and conformation, of loops in non-conserved regions create binding-site topographies that, complement the known solution conformations of their respective ligands., Thermodynamics interpreted in the light of structural information, highlights the differential role of water in the interaction of these CBMs, with their respective oligosaccharide ligands.
About this Structure
1GUI is a Single protein structure of sequence from Thermotoga maritima with BGC, CA and GOL as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Differential oligosaccharide recognition by evolutionarily-related beta-1,4 and beta-1,3 glucan-binding modules., Boraston AB, Nurizzo D, Notenboom V, Ducros V, Rose DR, Kilburn DG, Davies GJ, J Mol Biol. 2002 Jun 21;319(5):1143-56. PMID:12079353
Page seeded by OCA on Mon Nov 5 13:06:33 2007
Categories: Single protein | Thermotoga maritima | Davies, G.J. | Notenboom, V. | Nurizzo, D. | BGC | CA | GOL | Carbohydrate binding module | Cbm | Cellulose | Glucan
