Part:BBa_K4322005
CsgA-α (CsgA-Fibrin Knob Domain Fusion Protein)
CsgA is the polymer forming unit of the curli biogenesis pathway which leads to biofilm formation in Escherichia coli. The wild-type csgA monomer can already self-assemble to form homopolymers outside of the cell. However, for our hydrogel art this interaction lacks sufficient stability[2]. The mammalian protein fibrin arranges into fibrous chains to produce clots that hinder further blood loss. The polymerization of these chains relies on the interaction between N-terminal A- and B-knobs (alpha) and corresponding a- and b-holes (gamma) in the γ- and β-modules of fibrin[1]. When fused with protein csgA of the curli operon and chromoproteins, the fibrin knob domain (alpha) and the fibrin hole domain (gamma) will confer csgA the ability to stably crosslinking through the fibrin alpha and gamma domains.
References:
[1]R. I. Litvinov et al., “Polymerization of fibrin: direct observation and quantification of individual B:b knob-hole interactions,” Blood, vol. 109, no. 1, pp. 130–138, Jan. 2007, doi: 10.1182/blood-2006-07-033910.
[2]A. M. Duraj-Thatte et al., “Programmable microbial ink for 3D printing of living materials produced from genetically engineered protein nanofibers,” Nat Commun, vol. 12, no. 1, p. 6600, Dec. 2021, doi: 10.1038/s41467-021-26791-x.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 58
- 1000COMPATIBLE WITH RFC[1000]
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