Difference between revisions of "Part:BBa K2255018:Design"
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===Design Notes=== | ===Design Notes=== | ||
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+ | The domain 3 (D3) and the signal sequence are both the best conserved part from the attachment protein. Using a global protein alignment (Needleman-Wunsch and [https://static.igem.org/mediawiki/parts/5/52/T--Aix-Marseille--alignement.pdf MUSCLE alignments]), using two or three sequence at one time, we were eventually able to determinate domain 1 (D1) and domain 2 (D2) from XacF1. | ||
+ | We were able to found D1 and D2 domains because each domain is separated by a flexible sequence <ref>Heilpern, A. J. & Waldor, M. K. pIIICTX, a predicted CTXphi minor coat protein, can expand the host range of coliphage fd to include Vibrio cholerae. J. Bacteriol. 185, 1037–1044 (2003).</ref>. Then we retrotranslate this sequence in a nucleotidic sequence and we used iDT to optimise this sequence for ''E.coli'' production. | ||
===Source=== | ===Source=== |
Latest revision as of 14:28, 6 October 2017
p3_X.fuscans (Rfc25)
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12INCOMPATIBLE WITH RFC[12]Illegal NheI site found at 223
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Design Notes
The domain 3 (D3) and the signal sequence are both the best conserved part from the attachment protein. Using a global protein alignment (Needleman-Wunsch and MUSCLE alignments), using two or three sequence at one time, we were eventually able to determinate domain 1 (D1) and domain 2 (D2) from XacF1.
We were able to found D1 and D2 domains because each domain is separated by a flexible sequence [1]. Then we retrotranslate this sequence in a nucleotidic sequence and we used iDT to optimise this sequence for E.coli production.
Source
From the genomic sequence of XacF1.
References
- ↑ Heilpern, A. J. & Waldor, M. K. pIIICTX, a predicted CTXphi minor coat protein, can expand the host range of coliphage fd to include Vibrio cholerae. J. Bacteriol. 185, 1037–1044 (2003).