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Difference between revisions of "Carbohydrate Binding Module Family 19"

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== Structural Features ==
 
== Structural Features ==
Two alleles of the ''cts1'' gene have been identified, they are referred to as ''cts1-1'' and ''cts1-2'' <cite>Kuranda1991</cite>.  
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Two alleles of the ''cts1'' gene have been identified, they are referred to as ''cts1-1'' and ''cts1-2'' <cite>Kuranda1991</cite>.  The predicted full length protein is likely divided into four domains <cite>Kuranda1991</cite>. The first domain (amino acids 1-20) is the cleavable signal sequence, the second domain is the chitinase [[GHXX]] catalytic domain (amino acids 21-327), the third domain is a highly glycosylated serine/threonine-rich domain (amino acids 328-480) and the fourth domain is the high affinity chitin binding CBM19 <cite>Kuranda1991</cite>.  
  
  

Revision as of 03:46, 21 January 2021

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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/CBMnn.html

Ligand specificities

The CBM19 found in the CTS1 chitinase produced by Saccharomyces cerevisiae has been characterized as a chitin-binding CBM [1].

Mention here all major natural ligand specificities that are found within a given family (also plant or mammalian origin). Certain linkages and promiscuity would also be mentioned here if biologically relevant.

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: [2, 3]. CBMs, in particular, have been extensively reviewed [4, 5, 6, 7, 8].

Structural Features

Two alleles of the cts1 gene have been identified, they are referred to as cts1-1 and cts1-2 [1]. The predicted full length protein is likely divided into four domains [1]. The first domain (amino acids 1-20) is the cleavable signal sequence, the second domain is the chitinase GHXX catalytic domain (amino acids 21-327), the third domain is a highly glycosylated serine/threonine-rich domain (amino acids 328-480) and the fourth domain is the high affinity chitin binding CBM19 [1].


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

  • Fold: Structural fold (beta trefoil, beta sandwich, etc.)
  • 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

Chitin is an important component of the cell wall of Saccharomyces cerevisiae. It is specifically located at the junction of mother and daughter cells providing mechanical stability. The CTS1 enzyme produced by S. cerevisiae hydrolyses chitin [9, 10] and has a role in cell separation [1].


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
There is no 3D structural data on the CBM19 family.

References

  1. Kuranda MJ and Robbins PW. (1991). Chitinase is required for cell separation during growth of Saccharomyces cerevisiae. J Biol Chem. 1991;266(29):19758-67. | Google Books | Open Library PubMed ID:1918080 [Kuranda1991]
  2. Correa JU, Elango N, Polacheck I, and Cabib E. (1982). Endochitinase, a mannan-associated enzyme from Saccharomyces cerevisiae. J Biol Chem. 1982;257(3):1392-7. | Google Books | Open Library PubMed ID:6799506 [Correa1982]
  3. Kuranda MJ and Robbins PW. (1987). Cloning and heterologous expression of glycosidase genes from Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1987;84(9):2585-9. DOI:10.1073/pnas.84.9.2585 | PubMed ID:3033651 [Kuranda1987]

All Medline abstracts: PubMed