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Carbohydrate Binding Module Family 89

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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
http://www.cazy.org/CBM89.html

Ligand specificities

CBM89 is a small family that has been identified in bacteria. The CBM89 interaction with beechwood xylan and rye arabinoxylan was assessed using affinity gel electrophoresis (AGE) Cabral202Cabral202. Although similar β-helix structural organization has been found in GH28, GH91, PL6, and CE8, it was not observed any catalytic activity of the isolated CapCBM89 in the tested substrates Cabral202Cabral202.

Structural Features

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

  • Fold: The 1.85 Å CBM89 solved structure (retrieved from capybara gut metagenome) Cabral202Cabral202 displays a parallel β-helix fold, consisting of 14 complete helical turns.
  • Features of ligand binding: A Ca2+ was found in the structure, connecting the 11th and 12th turns (https://www.rcsb.org/structure/7JVI). The role of the ion seems to be only related to the domain stabilization, since a mutation in the Ca2+ binding site (D344L) affected the protein stability but not its capacity to bind to arabinoxylan/xylan Cabral202Cabral202. In CapCBM89, mutants Y62A and E82A impaired the capacity to bind to arabinoxylan/xylan, indicating the putative region for carbohydrate binding Cabral202Cabral202.

Functionalities

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

  • Functional role of CBM: In general, CBM89 might comprise approximately 600 to 1000 amino acids, which can be fused to GH domains. The CapCBM89 fused to a GH10 domain is inserted in a gene cluster targeting arabinoxylan Cabral202Cabral202. The cluster encodes the CapCBM89-GH10 and two exo-enzymes from GH43 and GH97 families <ref>Cabral2022<ref>. The GH10 domain is active on arabinoxylan and xylan, also suggesting that indeed the CapCBM89 might bind to these polysaccharides to assist GH10 catalysis in this case Cabral202Cabral202.
  • Most Common Associated Modules: 1. Glycoside Hydrolases from family GH10.


Family Firsts

First Identified The first CBM89 to be identified was from a MAG of Bacteroidaceae bacterium from the capybara gut microbiome Cabral202Cabral202.
First Structural Characterization The first CBM89 structure is the PDB ID 7JVI https://www.rcsb.org/structure/7JVI, retrieved from the capybara gut microbiome Cabral202Cabral202.

References

  1. pmid= 35110564

    [Cabral20222]