Part:BBa_K4728007

PhaF

Phasins, intracellular proteins, play a pivotal role in mediating the interaction between PHB (polyhydroxybutyrate) deposits and the cell through electrostatic interactions. Our selection of PhaF in our experiments was guided by literature, which underscores Pseudomonas' PhaF (Phasin F) as an optimal candidate for refinement. This is attributed to its well-defined PHB binding region on the N-terminal domain, with less reliance on the C-terminal domain. In this context, We employed the native PhaF for two key purposes: firstly, to evaluate its role in PHB binding, and secondly, to compare its binding capacity with our mutant PhaF.

BBa_K4728008 is an improved version of this part, having a higher binding affinity to PHB.

Sequence and Features

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  COMPATIBLE WITH RFC[12]
• 21
  INCOMPATIBLE WITH RFC[21]

  Illegal BglII site found at 71
  
• 23
  COMPATIBLE WITH RFC[23]
• 25
  INCOMPATIBLE WITH RFC[25]

  Illegal NgoMIV site found at 82
  Illegal NgoMIV site found at 630
  Illegal NgoMIV site found at 657
  Illegal NgoMIV site found at 672
  
• 1000
  COMPATIBLE WITH RFC[1000]

References

Maestro, Beatriz, et al. “A New Family of Intrinsically Disordered Proteins: Structural Characterization of the Major Phasin PhaF from Pseudomonas Putida KT2440.” PLoS ONE, vol. 8, no. 2, 15 Feb. 2013, p. e56904, https://doi.org/10.1371/journal.pone.0056904. Accessed 7 Feb. 2023.

Jendrossek, Dieter, and Daniel Pfeiffer. “New Insights in the Formation of Polyhydroxyalkanoate Granules (Carbonosomes) and Novel Functions of Poly(3-Hydroxybutyrate).” Environmental Microbiology, vol. 16, no. 8, 21 Jan. 2014, pp. 2357–2373, https://doi.org/10.1111/1462-2920.12356. Accessed 18 Nov. 2020.