Difference between revisions of "Carbohydrate Binding Module Family 76"

Revision as of 12:50, 13 May 2018

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.

Author: ^^^Ana Luis^^^
Responsible Curator: ^^^Harry Gilbert^^^

CAZy DB link
http://www.cazy.org/CBM76.html

Ligand specificities

CBM76 is a small family containing only five members found exclusively in Ruminococci. The founding member of this family is CBM76_RfGH44 from Ruminococcus flavefaciens that recognizes different β-1,4-glucans [1]. By isothermal titration calorimetry, the affinity of this binding module to xyloglucan (K_A 1.1 x 10⁶) is 100-fold higher than to glucomannan, barley β-glucan, hydroxyethylcellulose and XXXG (the repeating unit of xyloglucan, where X comprises glucose decorated at O6 with xylose and G corresponds to undecorated glucose) [1].

Structural Features

No three-dimensional structure has been solved for this CBM family.

Functionalities

The founding member of this family, CBM76_RfGH44, is appended to a glycoside hydrolase family 44 (GH44) and a C-terminal dockerin. The binding module specificity to β-1,4-glucans is consistent with the previously reported activity for GH44 enzymes (endoglucanase or xyloglucanase) [1]. However, the impact of CBM76_RfGH44 binding module on GH44 substrate recognition and catalysis it is not known.

Family Firsts

First Identified: CBM76_RfGH44 from Ruminococcus flavefaciens [1].
First Structural Characterization: No three-dimensional structure has been solved for this CBM family.

References

Venditto I, Luis AS, Rydahl M, Schückel J, Fernandes VO, Vidal-Melgosa S, Bule P, Goyal A, Pires VM, Dourado CG, Ferreira LM, Coutinho PM, Henrissat B, Knox JP, Baslé A, Najmudin S, Gilbert HJ, Willats WG, and Fontes CM. (2016). Complexity of the Ruminococcus flavefaciens cellulosome reflects an expansion in glycan recognition. Proc Natl Acad Sci U S A. 2016;113(26):7136-41. DOI:10.1073/pnas.1601558113 | PubMed ID:27298375 [Venditto2016]

@@ Line 17: / Line 17: @@
 == Ligand specificities ==
-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.
+CBM76 is a small family containing only five members found exclusively in Ruminococci. The founding member of this family is CBM76<sub>RfGH44</sub> from ''Ruminococcus flavefaciens'' that recognizes different β-1,4-glucans <cite>Venditto2016</cite>. By isothermal titration calorimetry, the affinity of this binding module to xyloglucan (K<sub>A</sub> 1.1 x 10<sup>6</sup>) is 100-fold higher than to glucomannan, barley β-glucan, hydroxyethylcellulose and XXXG (the repeating unit of xyloglucan, where X comprises glucose decorated at O6 with xylose and G corresponds to undecorated glucose) <cite>Venditto2016</cite>.
-''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: <cite>DaviesSinnott2008 Cantarel2009</cite>. CBMs, in particular, have been extensively reviewed <cite>Boraston2004 Hashimoto2006 Shoseyov2006 Guillen2010 Armenta2017</cite>.
 == Structural Features ==
-''Content in this section should include, in paragraph form, a description of:''
+No three-dimensional structure has been solved for this CBM family.
-* '''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 ==
-''Content in this section should include, in paragraph form, a description of:''
+The founding member of this family, CBM76<sub>RfGH44</sub>, is appended to a glycoside hydrolase family 44 ([[GH44]]) and a C-terminal dockerin. The binding module specificity to β-1,4-glucans is consistent with the previously reported activity for [[GH44]] enzymes (endoglucanase or xyloglucanase) <cite>Venditto2016</cite>. However, the impact of CBM76<sub>RfGH44</sub> binding module on [[GH44]] substrate recognition and catalysis it is not known.
-* '''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
+;First Identified:CBM76<sub>RfGH44</sub> from ''Ruminococcus flavefaciens'' <cite>Venditto2016</cite>.
-:Insert archetype here, possibly including ''very brief'' synopsis.
+;First Structural Characterization: No three-dimensional structure has been solved for this CBM family.
-;First Structural Characterization
-:Insert archetype here, possibly including ''very brief'' synopsis.
 == References ==
 <biblio>
-#Cantarel2009 pmid=18838391
+#Venditto2016 pmid=27298375
-#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].
-#Boraston2004 pmid=15214846
-#Hashimoto2006 pmid=17131061
-#Shoseyov2006 pmid=16760304
-#Guillen2010 pmid=19908036
-#Armenta2017 pmid=28547780
 </biblio>
 [[Category:Carbohydrate Binding Module Families|CBM076]]