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InterPro: IPR018366 Carbohydrate-binding type-2, conserved site
Protein matches
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UniProtKB Matches: 140 proteins |
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Accession
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IPR018366 CBM2_CS |
Type
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Conserved_site |
Signatures
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InterPro Relationships
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Found in
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IPR001919 Cellulose-binding domain, family II, bacterial type
IPR008965 Carbohydrate-binding
IPR012291 Cellulose-binding family II/chitobiase, carbohydrate-binding domain
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GO Term annotation
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Process
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GO:0005975 carbohydrate metabolic process
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Function
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GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0030246 carbohydrate binding
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InterPro annotation
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Entry Details in BioMart
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Abstract
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The microbial degradation of cellulose and xylans requires several types of enzyme such as endoglucanases (EC:3.2.1.4), cellobiohydrolases (EC:3.2.1.91) (exoglucanases), or xylanases (EC:3.2.1.8) [1].
Structurally, cellulases and xylanases generally consist of a catalytic domain joined to a cellulose-binding domain (CBD) by a short linker sequence rich in proline and/or hydroxy-amino acids.
The CBD domain is found either at the N-terminal or at the C-terminal extremity of these enzymes. As it is shown in the following schematic representation, there are two conserved cysteines in this CBD domain - one at each extremity of the domain - which have been shown [2] to be involved in a disulphide bond. There are also four conserved tryptophan, two are involved in cellulose binding.
The CBD of a number of bacterial cellulases has been shown to consist of about 105 amino acid residues [3, 4].
+-------------------------------------------------+
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xCxxxxWxxxxxNxxxWxxxxxxxWxxxxxxxxWNxxxxxGxxxxxxxxxxCx
'C': conserved cysteine involved in a disulphide bond.
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Structural links
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Database links
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Publications
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1.
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Gilkes NR, Henrissat B, Kilburn DG, Miller RC Jr, Warren RA.
Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families.
Microbiol. Rev. 55 303-15 1991
[PubMed: 1886523]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=1886523
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2.
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Gilkes NR, Claeyssens M, Aebersold R, Henrissat B, Meinke A, Morrison HD, Kilburn DG, Warren RA, Miller RC Jr.
Structural and functional relationships in two families of beta-1,4-glycanases.
Eur. J. Biochem. 202 367-77 1991
[PubMed: 1761039]
http://dx.doi.org/10.1111/j.1432-1033.1991.tb16384.x
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3.
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Meinke A, Gilkes NR, Kilburn DG, Miller RC Jr, Warren RA.
Bacterial cellulose-binding domain-like sequences in eucaryotic polypeptides.
Protein Seq. Data Anal. 4 349-53 1991
[PubMed: 1812490]
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4.
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Simpson PJ, Xie H, Bolam DN, Gilbert HJ, Williamson MP.
The structural basis for the ligand specificity of family 2 carbohydrate-binding modules.
J. Biol. Chem. 275 41137-42 2000
[PubMed: 10973978]
http://dx.doi.org/10.1074/jbc.M006948200
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Additional Reading
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Simpson PJ, Bolam DN, Cooper A, Ciruela A, Hazlewood GP, Gilbert HJ, Williamson MP.
A family IIb xylan-binding domain has a similar secondary structure to a homologous family IIa cellulose-binding domain but different ligand specificity.
Structure 7 1999 853-64
[PubMed: 10425686]
http://dx.doi.org/10.1016/S0969-2126(99)80108-7
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Nagy T, Simpson P, Williamson MP, Hazlewood GP, Gilbert HJ, Orosz L.
All three surface tryptophans in Type IIa cellulose binding domains play a pivotal role in binding both soluble and insoluble ligands.
FEBS Lett. 429 1998 312-6
[PubMed: 9662439]
http://dx.doi.org/10.1016/S0014-5793(98)00625-5
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Xu GY, Ong E, Gilkes NR, Kilburn DG, Muhandiram DR, Harris-Brandts M, Carver JP, Kay LE, Harvey TS.
Solution structure of a cellulose-binding domain from Cellulomonas fimi by nuclear magnetic resonance spectroscopy.
Biochemistry 34 1995 6993-7009
[PubMed: 7766609]
http://dx.doi.org/10.1021/bi00021a011
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InterPro 23.1
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