Difference between revisions of "Part:BBa K3889022"

Revision as of 22:09, 17 October 2021

Human Ovastacin protease phosphomimic_A

Since ovastacin (BBa_K3889024) has a eukaryotic origin, this protein undergoes several Post Translational Modifications (PTMs) including the addition of disulphide bonds and phosphorylation at serine and tyrosine residues. However, our recombinant protein will be produced in a prokaryotic organism which lacks the necessary genes to carry out PTMs. Hence, we used phosphomimetic variant(s) of ovastacin by changing or mutating the serine to aspartic acid and tyrosine to glutamic acid residues at S99, S156, S244 and Y279 (amino acid numbered with reference to pro-ovastacin) respectively. We then used I-TASSER to predict the structure of this phosphomimetic variant.

Protein Sequence

RLLSAASNKWPMGGDGVVEVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQRDFISIIPMYGCFSDVGRSGGMQVVSLAPTCLQKGRGIVLHELMHVLGFWHE HTRADRDRYIRVNWNEILPGFEINFIKSRSSNMLTPYDYSSVMHYGRLAFDRRGLPTITPLWAPSVHIGQRWNLSASDITRVLKLEGCS

Fig 3. Phosphomimetic variant of Ovastacin (aspartic acid residues marked with lime and glutamic acid residue marked with cyan)

C-score	Estimated TM-score	Estimated RMSD
1.84	0.97±0.05	1.8±1.5Å

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

@@ Line 3: / Line 3: @@
 <partinfo>BBa_K3889022 short</partinfo>
-Since ovastacin (<partinfo>BBa K3889024</partinfo>) has a eukaryotic origin, this protein undergoes several Post Translational Modifications (PTMs) including the addition of disulphide bonds and phosphorylation at serine and tyrosine residues.
+Since ovastacin (<partinfo>BBa_K3889024</partinfo>) has a eukaryotic origin, this protein undergoes several Post Translational Modifications (PTMs) including the addition of disulphide bonds and phosphorylation at serine and tyrosine residues.
 However, our recombinant protein will be produced in a prokaryotic organism which lacks the necessary genes to carry out PTMs. Hence, we used phosphomimetic variant(s) of ovastacin by changing or mutating the serine to aspartic acid and tyrosine to glutamic acid residues at S99, S156, S244 and Y279 (amino acid numbered with reference to pro-ovastacin) respectively. We then used I-TASSER to predict the structure of this phosphomimetic variant.