Cellulosomal scaffolding protein

Revision as of 13:44, 23 November 2014 by Yulia Baron (talk | contribs)

Carbohydrate Binding Module (Family 3 Clostridium Thermicellum)Carbohydrate Binding Module (Family 3 Clostridium Thermicellum)

Carbohydrate-binding domain modules(CBM) are non-catalytic domain which present in various microrganisms. [1]


Function

Carbohydrate-binding Module

The most important conformational element of most CBMs is the . t. The folds and architecture displayed by these beta-sheets have been classified into seven families with the β-sandwich being the most recurrent fold and the fold of family 3. [2]

Applications

The cellulose-binding module (CBM) is an attractive affinity tag for protein purification for several reasons:

1.Very specific binding ability to the fused protein eith CBM tag. 2.Very low nonspecific binding ability to to other protein. 3.efficient release of bound protein under nondenaturing conditions. [3]

Relevance

Structural highlights

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.


Caption for this structure

Drag the structure with the mouse to rotate

ReferencesReferences

  1. Guerreiro CI, Fontes CM, Gama M, Domingues L. Escherichia coli expression and purification of four antimicrobial peptides fused to a family 3 carbohydrate-binding module (CBM) from Clostridium thermocellum. Protein Expr Purif. 2008 May;59(1):161-8. doi: 10.1016/j.pep.2008.01.018. Epub, 2008 Feb 5. PMID:18328729 doi:http://dx.doi.org/10.1016/j.pep.2008.01.018
  2. Guillen D, Sanchez S, Rodriguez-Sanoja R. Carbohydrate-binding domains: multiplicity of biological roles. Appl Microbiol Biotechnol. 2010 Feb;85(5):1241-9. doi: 10.1007/s00253-009-2331-y., Epub 2009 Nov 12. PMID:19908036 doi:http://dx.doi.org/10.1007/s00253-009-2331-y
  3. Wan W, Wang D, Gao X, Hong J. Expression of family 3 cellulose-binding module (CBM3) as an affinity tag for recombinant proteins in yeast. Appl Microbiol Biotechnol. 2011 Aug;91(3):789-98. doi: 10.1007/s00253-011-3373-5., Epub 2011 Jun 9. PMID:21656139 doi:http://dx.doi.org/10.1007/s00253-011-3373-5

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Yulia Baron, Michal Harel, Jaime Prilusky