Difference between revisions of "Part:BBa K3409001"
Albane Mabro (Talk | contribs) |
|||
| Line 4: | Line 4: | ||
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. | 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 | ||
<!-- Add more about the biology of this part here | <!-- Add more about the biology of this part here | ||
| − | ===Usage | + | ===Usage=== |
<!-- --> | <!-- --> | ||
Latest revision as of 08:34, 26 October 2020
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
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 5
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 60
- 1000COMPATIBLE WITH RFC[1000]