Cellulosomal scaffolding protein: Difference between revisions
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== | == Carbohydrate Binding Module (Family 3 Clostridium Thermicellum)== | ||
<StructureSection load=' | <StructureSection load='1NBC' size='340' side='right' caption='Cellulosomal scaffolding protein A complex with Ca+2 ions (PDB code [[1nbc]])' scene=''> | ||
Carbohydrate-binding domain modules(CBM) are non-catalytic domain which present in glycoside hydrolases which target the associated catalytic modules to their substraes, therefore potentiating enzyme activietvarious microrganisms. CBM3 is part of CipA scafolding in Cellulosome which contain enzyme with hydrolytic activity(cellulase). <ref>doi:10.1016/j.pep.2008.01.018</ref> | |||
== Function == | == Function == | ||
CBM3 is Type A surface-binding-planar architecture of the binding sites is thought to be complementary to the flat surfaces presented by cellulose<ref>DOI 10.1042/BJ20040892</ref>. The binding site comprises a planar hydrophobic platform that contains three exposed aromatic amino acid | |||
The most important conformational element of most CBMs is the <scene name='60/609843/Beta_sheets/3'>Beta sheets</scene>. 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. <ref>DOI 10.1007/s00253-009-2331-y</ref>. And some <scene name='60/609843/Alpha_helics/1'>Alpha helics</scene>. | |||
== 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 non-denaturing conditions. <ref>doi:10.1007/s00253-011-3373-5</ref> | |||
== | == Structural highlights == | ||
== | This are some views of the Protein: This are some views of the Protein: <scene name='60/609843/Ball_and_stick/2'>Ball and stick</scene>, <scene name='60/609843/Spacefil/1'>Spacefill</scene>, <scene name='60/609843/Dots/1'>Dots</scene>, <scene name='60/609843/Strands/1'>Strands</scene> and <scene name='60/609843/Surface/3'>Surface</scene> presentation. | ||
== | ==3D structure of cellulosome scaffolding protein == | ||
[[Cellulosome scaffolding protein 3D structures]] | |||
</StructureSection> | |||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | |||
Latest revision as of 13:15, 2 May 2019
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 glycoside hydrolases which target the associated catalytic modules to their substraes, therefore potentiating enzyme activietvarious microrganisms. CBM3 is part of CipA scafolding in Cellulosome which contain enzyme with hydrolytic activity(cellulase). [1]
FunctionCBM3 is Type A surface-binding-planar architecture of the binding sites is thought to be complementary to the flat surfaces presented by cellulose[2]. The binding site comprises a planar hydrophobic platform that contains three exposed aromatic amino acid The most important conformational element of most CBMs is the . 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. [3]. And some . ApplicationsThe 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 non-denaturing conditions. [4] Structural highlightsThis are some views of the Protein: This are some views of the Protein: , , , and presentation. 3D structure of cellulosome scaffolding proteinCellulosome scaffolding protein 3D structures
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ReferencesReferences
- ↑ 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
- ↑ Boraston AB, Bolam DN, Gilbert HJ, Davies GJ. Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Biochem J. 2004 Sep 15;382(Pt 3):769-81. PMID:15214846 doi:http://dx.doi.org/10.1042/BJ20040892
- ↑ 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
- ↑ 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