Part:BBa_K3409001

Chaperone protein gp 38

For the proper folding of gp37, two chaperone proteins are required and have to be co-expressed, i.e., the gp 57a, encoded by the gene 57A and gp38, encoded by the gene 38. They both participate in the proper folding of the distal part of the long fibers.

Biology

In 2019, Islam et al. successfully over expressed the gp37(needle sequence), co-expressed with the chaperone proteins, in E. coli and purified it using the N-ter Histidine tag. The researchers conducted a binding assay by coating a plate with the LTF and putting it in contact with over expressed OmpC. They managed to show that there was no nonspecific binding and that the strength of binding of the LTF needle to the OmpC trimer depended on their concentration.

Bibliography

Islam, M. Z., Fokine, A., Mahalingam, M., Zhang, Z., Garcia-Doval, C., Van Raaij, M. J., Rossmann, M. G., & Rao, V. B. (2019). Molecular Anatomy of the Receptor Binding Module of a Bacteriophage Long Tail Fiber. PLoS Pathogens, 15(12), 1–21. https://doi.org/10.1371/journal.ppat.1008193

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 5
  
• 23
  COMPATIBLE WITH RFC[23]
• 25
  INCOMPATIBLE WITH RFC[25]

  Illegal AgeI site found at 60
  
• 1000
  COMPATIBLE WITH RFC[1000]