Part:BBa_K1462700:Design
GAL1+GBD+SH3+PDZ+PDZ+ADH1
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 615
Illegal BamHI site found at 648
Illegal BamHI site found at 820
Illegal BamHI site found at 1029
Illegal BamHI site found at 1352
Illegal BamHI site found at 1675
Illegal XhoI site found at 801
Illegal XhoI site found at 1010
Illegal XhoI site found at 1333
Illegal XhoI site found at 1656 - 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 150
- 1000COMPATIBLE WITH RFC[1000]
Design Notes
Scaffold protein, without Tom22, is a control group, #GBD: #SH3: #PDZ, 1:1:2. Without location, this part can fix the PRK, RuBisCO, CA to a limited space to increases the efficiency of interaction. In this way, We want to compare the effect of physicochemical property of Outer Membrane.
Source
The GBD,SH3,PDZ domain are synthesis from Genewiz. GAL1 and ADH1 is from the plate of IGEM.
References
[1] John E Dueber, Gabriel C Wu, G Reza Malmirchegini, et al.Synthetic protein scaffolds provide modular control over metabolic flux.Nat Biotechnol. 2009 Aug;27(8):753-9.
[2] Schultz, J. et al. Specific interactions between the syntrophin PDZ domain and voltage-gated sodium channels. Nat Struct Biol 5, 19-24 (1998).
[3] Kim, A.S., Kakalis, L.T., Abdul-Manan, N., Liu, G.A. & Rosen, M.K. Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. Nature 404, 151-158 (2000).
[4] Wu, X. et al. Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk. Structure 3, 215-226 (1995).
[5] Dueber, J.E., Yeh, B.J., Chak, K. & Lim, W.A. Reprogramming control of an allosteric signaling switch through modular recombination. Science 301, 1904-1908 (2003).