2G6E
Structure of cyclized F64L S65A Y66S GFP variant
Summary for 2G6E
| Entry DOI | 10.2210/pdb2g6e/pdb |
| Related | 1YJ2 2G16 2G2S 2G3D 2G5Z |
| Descriptor | Green fluorescent protein, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | chromophore, biosynthesis, post-translational modification, histidine ammonia lyase, mio, electrophile, luminescent protein |
| Biological source | Aequorea victoria |
| Total number of polymer chains | 1 |
| Total formula weight | 26755.34 |
| Authors | Barondeau, D.P. (deposition date: 2006-02-24, release date: 2006-04-18, Last modification date: 2024-10-30) |
| Primary citation | Barondeau, D.P.,Kassmann, C.J.,Tainer, J.A.,Getzoff, E.D. Understanding GFP Posttranslational Chemistry: Structures of Designed Variants that Achieve Backbone Fragmentation, Hydrolysis, and Decarboxylation. J.Am.Chem.Soc., 128:4685-4693, 2006 Cited by PubMed Abstract: The green fluorescent protein (GFP) creates a fluorophore out of three sequential amino acids by promoting spontaneous posttranslational modifications. Here, we use high-resolution crystallography to characterize GFP variants that not only undergo peptide backbone cyclization but additional denaturation-induced peptide backbone fragmentation, native peptide hydrolysis, and decarboxylation reactions. Our analyses indicate that architectural features that favor GFP peptide cyclization also drive peptide hydrolysis. These results are relevant for the maturation pathways of GFP homologues, such as the kindling fluorescent protein and the Kaede protein, which use backbone cleavage to red-shift the spectral properties of their chromophores. We further propose a photochemical mechanism for the decarboxylation reaction, supporting a role for the GFP protein environment in facilitating radical formation and one-electron chemistry, which may be important in activating oxygen for the oxidation step of chromophore biosynthesis. Together, our results characterize GFP posttranslational modification chemistry with implications for the energetic landscape of backbone cyclization and subsequent reactions, and for the rational design of predetermined spontaneous backbone cyclization and cleavage reactions. PubMed: 16594705DOI: 10.1021/ja056635l PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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