D
IPR002044

Carbohydrate binding module family 20

InterPro entry
Short nameCBM20
Overlapping
homologous
superfamilies
 
domain relationships

Description

This entry represents
CBM20
, which binds starch. The crystal structure of CBM20 has been solved
[3]
. It consists of seven β-strands forming an open-sided distorted β-barrel. Several aromatic residues, especially the well-conserved Trp and Tyr residues, participate in granular starch binding.

A carbohydrate-binding module (CBM) is defined as a contiguous amino acid sequence within a carbohydrate-active enzyme with a discreet fold having carbohydrate-binding activity. A few exceptions are CBMs in cellulosomal scaffolding proteins and rare instances of independent putative CBMs. The requirement of CBMs existing as modules within larger enzymes sets this class of carbohydrate-binding protein apart from other non-catalytic sugar binding proteins such as lectins and sugar transport proteins.

CBMs were previously classified as cellulose-binding domains (CBDs) based on the initial discovery of several modules that bound cellulose
[4, 2]
. However, additional modules in carbohydrate-active enzymes are continually being found that bind carbohydrates other than cellulose yet otherwise meet the CBM criteria, hence the need to reclassify these polypeptides using more inclusive terminology.

Previous classification of cellulose-binding domains were based on amino acid similarity. Groupings of CBDs were called "Types" and numbered with roman numerals (e.g. Type I or Type II CBDs). In keeping with the glycoside hydrolase classification, these groupings are now called families and numbered with Arabic numerals. Families 1 to 13 are the same as Types I to XIII. For a detailed review on the structure and binding modes of CBMs see
[1]
.

References

1.Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Boraston AB, Bolam DN, Gilbert HJ, Davies GJ. Biochem. J. 382, 769-81, (2004). PMID: 15214846

2.Precise excision of the cellulose binding domains from two Cellulomonas fimi cellulases by a homologous protease and the effect on catalysis. Gilkes NR, Warren RA, Miller RC Jr, Kilburn DG. J. Biol. Chem. 263, 10401-7, (1988). PMID: 3134347

3.Structure of cyclodextrin glycosyltransferase refined at 2.0 A resolution. Klein C, Schulz GE. J. Mol. Biol. 217, 737-50, (1991). View articlePMID: 1826034

4.Studies of the cellulolytic system of Trichoderma reesei QM 9414. Analysis of domain function in two cellobiohydrolases by limited proteolysis. Tomme P, Van Tilbeurgh H, Pettersson G, Van Damme J, Vandekerckhove J, Knowles J, Teeri T, Claeyssens M. Eur. J. Biochem. 170, 575-81, (1988). View articlePMID: 3338453

GO terms

biological process

  • None

molecular function

cellular component

  • None

Cross References

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