6AS9
Filamentous Assembly of Green Fluorescent Protein Supported by a C-terminal fusion of 18-residues, viewed in space group P212121 form 2
Summary for 6AS9
| Entry DOI | 10.2210/pdb6as9/pdb |
| Related | 5HBD 5HGE 5HW9 |
| Descriptor | Green fluorescent protein, ACETATE ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total) |
| Functional Keywords | filament, protofilament, 2 sub 1 screw symmetry, protein fibril |
| Biological source | Aequorea victoria (Jellyfish) |
| Total number of polymer chains | 1 |
| Total formula weight | 29305.06 |
| Authors | Sawaya, M.R.,Heller, D.M.,McPartland, L.,Hochschild, A.,Eisenberg, D.S. (deposition date: 2017-08-23, release date: 2018-05-30, Last modification date: 2025-04-02) |
| Primary citation | McPartland, L.,Heller, D.M.,Eisenberg, D.S.,Hochschild, A.,Sawaya, M.R. Atomic insights into the genesis of cellular filaments by globular proteins. Nat. Struct. Mol. Biol., 25:705-714, 2018 Cited by PubMed Abstract: Self-assembly of proteins into filaments, such as actin and tubulin filaments, underlies essential cellular processes in all three domains of life. The early emergence of filaments in evolutionary history suggests that filament genesis might be a robust process. Here we describe the fortuitous construction of GFP fusion proteins that self-assemble as fluorescent polar filaments in Escherichia coli. Filament formation is achieved by appending as few as 12 residues to GFP. Crystal structures reveal that each protomer donates an appendage to fill a groove between the two following protomers along the filament. This exchange of appendages resembles runaway domain swapping but is distinguished by higher efficiency because monomers cannot competitively bind their own appendages. Ample evidence for this 'runaway domain coupling' mechanism in nature suggests it could facilitate the evolutionary pathway from globular protein to polar filament, requiring a minimal extension of protein sequence and no substantial refolding. PubMed: 30076408DOI: 10.1038/s41594-018-0096-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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