6S68
Structure of the Fluorescent Protein AausFP2 from Aequorea cf. australis at pH 7.6
Summary for 6S68
| Entry DOI | 10.2210/pdb6s68/pdb |
| Descriptor | Aequorea cf. australis fluorescent protein 2 (AausFP2) (2 entities in total) |
| Functional Keywords | gfp-like fluorescent protein, fluorescent protein |
| Biological source | Aequorea australis |
| Total number of polymer chains | 1 |
| Total formula weight | 25571.07 |
| Authors | Depernet, H.,Gotthard, G.,Lambert, G.G.,Shaner, N.C.,Royant, A. (deposition date: 2019-07-02, release date: 2020-07-22, Last modification date: 2024-01-24) |
| Primary citation | Lambert, G.G.,Depernet, H.,Gotthard, G.,Schultz, D.T.,Navizet, I.,Lambert, T.,Adams, S.R.,Torreblanca-Zanca, A.,Chu, M.,Bindels, D.S.,Levesque, V.,Nero Moffatt, J.,Salih, A.,Royant, A.,Shaner, N.C. Aequorea's secrets revealed: New fluorescent proteins with unique properties for bioimaging and biosensing. Plos Biol., 18:e3000936-e3000936, 2020 Cited by PubMed Abstract: Using mRNA sequencing and de novo transcriptome assembly, we identified, cloned, and characterized 9 previously undiscovered fluorescent protein (FP) homologs from Aequorea victoria and a related Aequorea species, with most sequences highly divergent from A. victoria green fluorescent protein (avGFP). Among these FPs are the brightest green fluorescent protein (GFP) homolog yet characterized and a reversibly photochromic FP that responds to UV and blue light. Beyond green emitters, Aequorea species express purple- and blue-pigmented chromoproteins (CPs) with absorbances ranging from green to far-red, including 2 that are photoconvertible. X-ray crystallography revealed that Aequorea CPs contain a chemically novel chromophore with an unexpected crosslink to the main polypeptide chain. Because of the unique attributes of several of these newly discovered FPs, we expect that Aequorea will, once again, give rise to an entirely new generation of useful probes for bioimaging and biosensing. PubMed: 33137097DOI: 10.1371/journal.pbio.3000936 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.06 Å) |
Structure validation
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