Difference between revisions of "Part:BBa K1583102"

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CsgA is a protein monomer which can aggregate to form amyloid nanowires in natural biofilms of <i>E.coli</i>. This protein is transported as an unfolded protein out of the cell. Outside the cell CsgA proteins self-assemble into nanowires after nucleation on the membrane protein CsgB. CsgC prevents CsgA proteins from self-assembling inside the cell and the transport is ensured by the proteins CsgEFG.
 
CsgA is a protein monomer which can aggregate to form amyloid nanowires in natural biofilms of <i>E.coli</i>. This protein is transported as an unfolded protein out of the cell. Outside the cell CsgA proteins self-assemble into nanowires after nucleation on the membrane protein CsgB. CsgC prevents CsgA proteins from self-assembling inside the cell and the transport is ensured by the proteins CsgEFG.
  
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This part generates a peptide tag which shows high adhesive properties towards hydroxyapatite, a main component of e.g. teeth. (Roy et al. 2008)
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This part generates a peptide tag which shows high adhesive properties towards hydroxyapatite, a main component of e.g. teeth. The sequence of the hydroxyapatite-binding peptide is from an article by Roy et al. 2008.
  
 
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<span class='h3bb'>Sequence and Features</span>
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<span class='h3bb'><h3>Sequence and Features</h3></span>
 
<partinfo>BBa_K1583102 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K1583102 SequenceAndFeatures</partinfo>
  
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Reference
 
Reference
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<p>Roy, M.D. et al., 2008. Identification of a Highly Specific Hydroxyapatite-binding Peptide using Phage Display. Advanced Materials, 20(10), pp.1830–1836.</p>
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<p>Roy, M. D., Stanley, S. K., Amis, E. J., & Becker, M. L. (2008). Identification of a Highly Specific Hydroxyapatite-binding Peptide using Phage Display. Advanced Materials, 20(10), 1830–1836. p>
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Revision as of 15:00, 18 September 2015

pRha + CsgA + Hydroxyapatite-affinity tag

CsgA with Hydroxyapatite-tag attachted to the C-terminus under control of L-rhamnose-inducible promoter ((BBa_K914003). CsgA is a protein monomer which can aggregate to form amyloid nanowires in natural biofilms of E.coli. This protein is transported as an unfolded protein out of the cell. Outside the cell CsgA proteins self-assemble into nanowires after nucleation on the membrane protein CsgB. CsgC prevents CsgA proteins from self-assembling inside the cell and the transport is ensured by the proteins CsgEFG. This part generates a peptide tag which shows high adhesive properties towards hydroxyapatite, a main component of e.g. teeth. The sequence of the hydroxyapatite-binding peptide is from an article by Roy et al. 2008.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Reference

Roy, M. D., Stanley, S. K., Amis, E. J., & Becker, M. L. (2008). Identification of a Highly Specific Hydroxyapatite-binding Peptide using Phage Display. Advanced Materials, 20(10), 1830–1836. p>