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| Oligomerization | Organism | Molecular Weight | Cofactor |
|---|---|---|---|
| Monomer | Clavularia sp. | 27.0 kDa | - |
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mClavGR1 was derived from mTFP1 with the following mutations: G44S/K55R/E72S/Y76F/D77E/N80Q/N83D/S95A/A104H/A109V/N119D/T134S/K140G/V143C/K144I/V145A/K146T/S147N/S150T/E153K/Y158N/E159K/L162F/T179V/D182E/R187K/H201M/E206K/H211Y/V213C/K216R/I218T/R220K/K222_K223insQ/N241S/T250K/V251L/S254H/R258H/N259S/S260G/T261L/D261aP
amino acid numbers relative to cFP484. show relative to mTFP1
Note: Note: Supp. Table 1 in Hoi et al (2010) does not list mTFP1-T141V (position relative to mTFP1 as shown in paper) as one of the mutations in mClavGR1. But Fig. 2 in the paper shows all mClavGR proteins with 141V. It is included in the sequence and mutation list here (as T146V relative to mTFP1).
The new photoconvertible FP based on the mTFP*1 template was designed using a strategy analogous to that previously used to design a consensus FP based on a monomeric Azami green template.25 The known photoconvertible FPs, including EosFP, Dendra2, KikGR, and Kaede were aligned to find the consensus at each amino acid position. Amino acids of > 50% consensus were maintained in the designed protein. At positions with no clear consensus, the corresponding residue in mTFP*1 was used. Residues of mTFP*1 that had been substituted during the conversion of the wild-type cFP484 tetramer into a monomer were maintained in the design of the consensus protein
Hoi et al. (2010)
(2010). Journal of Molecular Biology, 401(5) , 776-791. doi: 10.1016/j.jmb.2010.06.056. Article Pubmed
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