6DEJ
The structure of HcRed7, a brighter and red-shifted HcRed variant
Summary for 6DEJ
| Entry DOI | 10.2210/pdb6dej/pdb |
| Descriptor | GFP-like non-fluorescent chromoprotein, SULFATE ION, DODECAETHYLENE GLYCOL, ... (5 entities in total) |
| Functional Keywords | hcred, red, far-red, fluorescent protein |
| Biological source | Heteractis crispa (Leathery sea anemone) |
| Total number of polymer chains | 4 |
| Total formula weight | 108107.94 |
| Authors | Wannier, T.M.,Mayo, S.L. (deposition date: 2018-05-12, release date: 2018-05-23, Last modification date: 2024-10-23) |
| Primary citation | Wannier, T.M.,Gillespie, S.K.,Hutchins, N.,McIsaac, R.S.,Wu, S.Y.,Shen, Y.,Campbell, R.E.,Brown, K.S.,Mayo, S.L. Monomerization of far-red fluorescent proteins. Proc. Natl. Acad. Sci. U.S.A., 115:E11294-E11301, 2018 Cited by PubMed Abstract: -class red fluorescent proteins (RFPs) are frequently used as biological markers, with far-red (λ ∼ 600-700 nm) emitting variants sought for whole-animal imaging because biological tissues are more permeable to light in this range. A barrier to the use of naturally occurring RFP variants as molecular markers is that all are tetrameric, which is not ideal for cell biological applications. Efforts to engineer monomeric RFPs have typically produced dimmer and blue-shifted variants because the chromophore is sensitive to small structural perturbations. In fact, despite much effort, only four native RFPs have been successfully monomerized, leaving the majority of RFP biodiversity untapped in biomarker development. Here we report the generation of monomeric variants of HcRed and mCardinal, both far-red dimers, and describe a comprehensive methodology for the monomerization of red-shifted oligomeric RFPs. Among the resultant variants is mKelly1 (emission maximum, λ = 656 nm), which, along with the recently reported mGarnet2 [Matela G, et al. (2017) 53:979-982], forms a class of bright, monomeric, far-red FPs. PubMed: 30425172DOI: 10.1073/pnas.1807449115 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6279 Å) |
Structure validation
Download full validation report
