5LTR
Structure of the Yellow-Green Fluorescent Protein mNeonGreen from Branchiostoma lanceolatum at the near physiological pH 8.0
Summary for 5LTR
| Entry DOI | 10.2210/pdb5ltr/pdb |
| Descriptor | mNeonGreen, CHLORIDE ION (3 entities in total) |
| Functional Keywords | fluorescent protein |
| Biological source | Branchiostoma lanceolatum (Common lancelet) |
| Total number of polymer chains | 1 |
| Total formula weight | 30731.69 |
| Authors | Clavel, D.,Gotthard, G.,Royant, A. (deposition date: 2016-09-07, release date: 2016-12-07, Last modification date: 2024-01-17) |
| Primary citation | Clavel, D.,Gotthard, G.,von Stetten, D.,De Sanctis, D.,Pasquier, H.,Lambert, G.G.,Shaner, N.C.,Royant, A. Structural analysis of the bright monomeric yellow-green fluorescent protein mNeonGreen obtained by directed evolution. Acta Crystallogr D Struct Biol, 72:1298-1307, 2016 Cited by PubMed Abstract: Until recently, genes coding for homologues of the autofluorescent protein GFP had only been identified in marine organisms from the phyla Cnidaria and Arthropoda. New fluorescent-protein genes have now been found in the phylum Chordata, coding for particularly bright oligomeric fluorescent proteins such as the tetrameric yellow fluorescent protein lanYFP from Branchiostoma lanceolatum. A successful monomerization attempt led to the development of the bright yellow-green fluorescent protein mNeonGreen. The structures of lanYFP and mNeonGreen have been determined and compared in order to rationalize the directed evolution process leading from a bright, tetrameric to a still bright, monomeric fluorescent protein. An unusual discolouration of crystals of mNeonGreen was observed after X-ray data collection, which was investigated using a combination of X-ray crystallography and UV-visible absorption and Raman spectroscopies, revealing the effects of specific radiation damage in the chromophore cavity. It is shown that X-rays rapidly lead to the protonation of the phenolate O atom of the chromophore and to the loss of its planarity at the methylene bridge. PubMed: 27917830DOI: 10.1107/S2059798316018623 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.21 Å) |
Structure validation
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