7LG4
Green fluorescent protein from Aequorea macrodactyla - amacGFP
Summary for 7LG4
| Entry DOI | 10.2210/pdb7lg4/pdb |
| Descriptor | Green fluorescent protein, 1,2-ETHANEDIOL, DI(HYDROXYETHYL)ETHER, ... (5 entities in total) |
| Functional Keywords | fluorescent protein |
| Biological source | Aequorea macrodactyla |
| Total number of polymer chains | 1 |
| Total formula weight | 28356.13 |
| Authors | Bozhanova, N.G.,Meiler, J. (deposition date: 2021-01-19, release date: 2021-01-27, Last modification date: 2024-11-20) |
| Primary citation | Gonzalez Somermeyer, L.,Fleiss, A.,Mishin, A.S.,Bozhanova, N.G.,Igolkina, A.A.,Meiler, J.,Alaball Pujol, M.E.,Putintseva, E.V.,Sarkisyan, K.S.,Kondrashov, F.A. Heterogeneity of the GFP fitness landscape and data-driven protein design. Elife, 11:-, 2022 Cited by PubMed Abstract: Studies of protein fitness landscapes reveal biophysical constraints guiding protein evolution and empower prediction of functional proteins. However, generalisation of these findings is limited due to scarceness of systematic data on fitness landscapes of proteins with a defined evolutionary relationship. We characterized the fitness peaks of four orthologous fluorescent proteins with a broad range of sequence divergence. While two of the four studied fitness peaks were sharp, the other two were considerably flatter, being almost entirely free of epistatic interactions. Mutationally robust proteins, characterized by a flat fitness peak, were not optimal templates for machine-learning-driven protein design - instead, predictions were more accurate for fragile proteins with epistatic landscapes. Our work paves insights for practical application of fitness landscape heterogeneity in protein engineering. PubMed: 35510622DOI: 10.7554/eLife.75842 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.81 Å) |
Structure validation
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