Protein_Domain
eCPX-nSA-c

Part:BBa_M50000:Design

Designed by: Nicolas Quach   Group: Stanford BIOE44 - S11   (2016-10-24)


Streptavidin binding outer membrane protein


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]


Design Notes

eCPX was developed as a biterminal display scaffold, and thus both N and C termini are available for fusion with other domains. An N terminal fusion with a streptavidin binding domain had already been created by Rice and Daugherty for their paper on eCPX; we wished to increase the affinity by fusing another (stronger binding) streptavidin binding domain to the C terminus. We decided to use the 15 residue Nanotag (developed by Lamla and Erdmann) as the C terminal streptavidin binding domain. In order to fuse Nanotag to the C terminus, we added a 6 amino acid serine glycine linker to separate eCPX from Nanotag, to prevent misfolding due to steric effects.

Source

Derived from E. coli outer membrane protein OmpX. eCPX is an engineered version of OmpX developed by Rice and Daugherty (Protein Eng. Des. Sel., 2008, pg 435-442)

References