Family 6 carbohydrate-binding modules display multiple beta1,3-linked glucan-specific binding interfaces
| Autor: | Márcia A.S. Correia, José A.M. Prates, VirgÃnia M.R. Pires, David N. Bolam, Vânia O. Fernandes, Carlos M. G. A. Fontes, Victor D. Alves, Harry J. Gilbert, L M A Ferreira |
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| Rok vydání: | 2009 |
| Předmět: |
Stereochemistry
Cellvibrio Molecular Sequence Data Receptors Cell Surface Microbiology Substrate Specificity Bacterial Proteins Genetics Protein–carbohydrate interactions Binding site Molecular Biology Glucans Glucan chemistry.chemical_classification Binding Sites biology Sequence Homology Amino Acid Carbohydrate biology.organism_classification Enzyme chemistry Biochemistry Multigene Family Bacillus halodurans Sequence Alignment Pseudomonadaceae Protein Binding |
| Zdroj: | FEMS microbiology letters. 300(1) |
| ISSN: | 1574-6968 |
| Popis: | Noncatalytic carbohydrate-binding modules (CBMs), which are found in a variety of carbohydrate-degrading enzymes, have been grouped into sequence-based families. CBMs, by recruiting their appended enzymes onto the surface of the target substrate, potentiate catalysis particularly against insoluble substrates. Family 6 CBMs (CBM6s) display unusual properties in that they present two potential ligand-binding sites termed clefts A and B, respectively. Cleft B is located on the concave surface of the beta-sandwich fold while cleft A, the more common binding site, is formed by the loops that connect the inner and the outer beta-sheets. Here, we report the biochemical properties of CBM6-1 from Cellvibrio mixtus CmCel5A. The data reveal that CBM6-1 specifically recognizes beta1,3-glucans through residues located both in cleft A and in cleft B. In contrast, a previous report showed that a CBM6 derived from a Bacillus halodurans laminarinase binds to beta1,3-glucans only in cleft A. These studies reveal a different mechanism by which a highly conserved protein platform can recognize beta1,3-glucans. |
| Databáze: | OpenAIRE |
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