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Carbohydrate Binding Module Family 6

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Revision as of 00:12, 20 December 2013 by Mirjam Czjzek (talk | contribs)
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This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.


CAZy DB link
https://www.cazy.org/CBM6.html

Ligand specificities

The ligand specificity of the first characterized CBM6, originating from a multimodular xylanase from Clostridium thermocellum, was determined to be xylan [1], although the results showed that this CBM6 was also able to bind to Avicel and acid-swollen cellulose. This was also the first CBM6 for which a 3D structure was determined [2], and multiple sequence alignments, analyzed in the light of the first 3D structure, already gave clear indications that large diversity in specificity was to be expected among CBM6 modules [2]. CBM6 modules are in general attached to bacterial or archeal polysaccharide degrading enzymes and can be found attached to xylanases, cellulases, agarases, laminarinases, etc [3]. Interestingly, modules assigned to the CBM6 family have also been found associated to fungal enzymes and to the α-subunit of the coagulation factor G in horseshoe crabs eukarotic CBM6 occurence. In the latter case, the β-1,3-glucan binding of the C-terminal tandem CBM6s has been demonstrated [4]. Those CBM6s having characterized binding activities cover : both linear and branched/decorated xylan, β-1,4-glucan (or cellulose), mixed-linked β-1,3-1,4-glucan (or lichenan), agarose, β-1,3-glucan (or laminarin) and chitin. Remarkably, the characterization and 3D structure of a CBM6 from Cellvibrio mixtus revealed two distinct binding sites that displayed differential binding specificities [5, 6].

Note: Here is an example of how to insert references in the text, together with the "biblio" section below: Please see these references for an essential introduction to the CAZy classification system: [7, 8]. CBMs, in particular, have been extensively reviewed [9, 10, 11, 12].

Structural Features

Content in this section should include, in paragraph form, a description of:

  • Fold: Likewise many other CBMs, the overall fold corresponds to a β-sandwich, but the first identified ligand binding site was not, as usual, located at a shallow cleft on the concave surface of the β-sheets (cleft B in CBM6). Alternatively, a binding site was found located within the connecting loops of the two β-sheets (cleft A in CBM6). Interestingly, some CBM6s display binding affinities for both binding sites,
  • Type: Include here Type A, B, or C and properties
  • Features of ligand binding: Describe CBM binding pocket location (Side or apex) important residues for binding (W, Y, F, subsites), interact with reducing end, non-reducing end, planar surface or within polysaccharide chains. Include examples pdb codes. Metal ion dependent. Etc.

Functionalities

Content in this section should include, in paragraph form, a description of:

  • Functional role of CBM: Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.
  • Most Common Associated Modules: 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)
  • Novel Applications: Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.

Family Firsts

First Identified
Insert archetype here, possibly including very brief synopsis.
First Structural Characterization
Insert archetype here, possibly including very brief synopsis.

References

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  1. Error fetching PMID 10432306: [Fernandes1999]
  2. Error fetching PMID 11673472: [Czjzek2001]
  3. Error fetching PMID 19240276: [Michel2009]
  4. Error fetching PMID 11830593: [Takaki2002]
  5. Error fetching PMID 15004011: [Henshaw2004]
  6. Error fetching PMID 15010454: [Pires2004]
  7. [15004011]

All Medline abstracts: PubMed