Carbohydrate Binding Module Family 63

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.

• Authors: ^^^William R. Chase and Daniel J. Cosgrove^^^
• Responsible Curator: ^^^Daniel J. Cosgrove^^^

---

CAZy DB link

http://www.cazy.org/CBM63.html

Introduction

In nature, CBM63 is found almost exclusively as the C-terminal domain of the two-domain protein named expansin. Expansins are ubiquitous in plants where they function in cell growth and other developmental processes that involve plant cell wall modification ADDIN EN.CITE ADDIN EN.CITE.DATA [1,2] . They are also present in diverse microbes, including many bacterial and fungal plant pathogens ADDIN EN.CITE <EndNote>[1, 1, 2, 2, 3, 3, 4, 4, 5, 5, 6, 6, 6, 7, 7, 8, 9, 9, 10, 10, 11, 11, 12, 12, 12, 12, 13, 13, 14, 14, 14, 14, 14, 14, 14, 14, 14, 14, 14, 14, 15, 16, 16, 17, 18, 19, 20, 21, 22, 22, 23, 24, 25, 26, 27, 27, 28, 28, 29, 29, 30, 31, 32, 32, 33, 34, 35, 36, 36, 37, 38, 38, 39, 40, 41, 42, 43, 44, 45, 45, 46, 46, 47, 48, 49, 49, 50, 50, 51, 51, 52, 52, 53, 53, 54, 54, 55, 55, 56, 57, 57, 58, 59, 59, 60, 60, 60, 60, 60, 60, 60, 60, 60, 60, 60, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 71, 72, 72, 73, 73, 74, 74, 75, 76, 77, 77, 78, 79, 80, 81, 82, 83, 83, 84, 84, 85, 85, 86, 86, 87, 87, 87, 87, 88, 89, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 100, 101, 101, 102, 102, 103, 103]</EndNote>[3]. Microbes may have acquired expansin genes via horizontal gene transfer(s) from plants in the distant past ADDIN EN.CITE <EndNote>[1, 1, 2, 3, 3, 5, 5, 7, 7, 9, 9, 10, 10, 11, 11, 12, 12, 12, 12, 13, 13, 14, 14, 14, 14, 14, 14, 14, 14, 14, 14, 14, 14, 15, 16, 16, 17, 18, 20, 21, 22, 22, 23, 24, 25, 26, 27, 27, 28, 28, 29, 29, 29, 29, 29, 29, 30, 31, 32, 32, 33, 34, 35, 37, 38, 45, 45, 46, 46, 49, 49, 53, 53, 54, 54, 54, 54, 55, 55, 57, 57, 71, 71, 72, 72, 73, 73, 74, 74, 77, 77, 79, 80, 82, 83, 83, 85, 85, 86, 86, 87, 87, 87, 87, 89, 90, 91, 92, 93, 94, 95, 95, 97, 99, 100, 103, 103, 104, 104, 105, 105, 106, 106, 106, 107, 108, 109, 109, 110, 111, 112, 113, 113, 113, 113, 113, 114, 115, 116, 117, 118, 119, 120, 121, 122, 123, 124, 125, 126, 126, 127, 128, 129, 130, 131, 132, 133, 134, 134, 135, 135, 136, 136, 137, 137, 138, 138, 139, 140, 140, 141, 142, 143, 143, 144, 144, 145, 145, 146, 147, 148, 149, 149, 150, 151, 152, 153, 154, 155, 156, 157]</EndNote>[4]. The founding member of CBM63 is based on the C-terminal domain of the expansin designated BsEXLX1 from the soil bacterium Bacillus subtilis ADDIN EN.CITE ADDIN EN.CITE.DATA [5] . It contains ~100 amino acids with a total relative MW of ~11.5 kDa. In the current CAZypedia database, plant sequences are not included in the CBM63 listings, a consequence of the large sequence divergence of expansins and limitations of automated sequence-based methods used to construct CBM families. However, structural analysis leaves little doubt of the homology between plant and bacterial expansins ADDIN EN.CITE ADDIN EN.CITE.DATA [6] , including the C-terminal domain identified as CBM63 in numerous microbial expansins.

Structural Features

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

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

158. Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, and Henrissat B. (2009). The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009;37(Database issue):D233-8. DOI:10.1093/nar/gkn663 |

159. 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. Download PDF version.

160. Boraston AB, Bolam DN, Gilbert HJ, and Davies GJ. (2004). Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Biochem J. 2004;382(Pt 3):769-81. DOI:10.1042/BJ20040892 |
161. Hashimoto H (2006). Recent structural studies of carbohydrate-binding modules. Cell Mol Life Sci. 2006;63(24):2954-67. DOI:10.1007/s00018-006-6195-3 |
162. Shoseyov O, Shani Z, and Levy I. (2006). Carbohydrate binding modules: biochemical properties and novel applications. Microbiol Mol Biol Rev. 2006;70(2):283-95. DOI:10.1128/MMBR.00028-05 |
163. Guillén D, Sánchez S, and Rodríguez-Sanoja R. (2010). Carbohydrate-binding domains: multiplicity of biological roles. Appl Microbiol Biotechnol. 2010;85(5):1241-9. DOI:10.1007/s00253-009-2331-y |