Summary for 6YFE
| Entry DOI | 10.2210/pdb6yfe/pdb |
| Related | 6YF7 6YF9 6YFA 6YFB 6YFC 6YFD 6YFF 6YFG 6YFH 6YFI 6YFJ 6YFK 6YFL 6YFM 6YFN 6YFO 6YFP 6YFQ 6YFR 6YFS 6YFT 6YFU |
| Descriptor | coat protein, CALCIUM ION (2 entities in total) |
| Functional Keywords | virus, virus-like particle, structural protein, virus like particle |
| Biological source | Beihai levi-like virus 19 |
| Total number of polymer chains | 90 |
| Total formula weight | 1293705.66 |
| Authors | Rumnieks, J.,Kalnins, G.,Sisovs, M.,Lieknina, I.,Tars, K. (deposition date: 2020-03-26, release date: 2020-09-02, Last modification date: 2024-01-24) |
| Primary citation | Rumnieks, J.,Lieknina, I.,Kalnins, G.,Sisovs, M.,Akopjana, I.,Bogans, J.,Tars, K. Three-dimensional structure of 22 uncultured ssRNA bacteriophages: Flexibility of the coat protein fold and variations in particle shapes. Sci Adv, 6:-, 2020 Cited by PubMed Abstract: The single-stranded RNA (ssRNA) bacteriophages are among the simplest known viruses with small genomes and exceptionally high mutation rates. The number of ssRNA phage isolates has remained very low, but recent metagenomic studies have uncovered an immense variety of distinct uncultured ssRNA phages. The coat proteins (CPs) in these genomes are particularly diverse, with notable variation in length and often no recognizable similarity to previously known viruses. We recombinantly expressed metagenome-derived ssRNA phage CPs to produce virus-like particles and determined the three-dimensional structure of 22 previously uncharacterized ssRNA phage capsids covering nine distinct CP types. The structures revealed substantial deviations from the previously known ssRNA phage CP fold, uncovered an unusual prolate particle shape, and revealed a previously unseen dsRNA binding mode. These data expand our knowledge of the evolution of viral structural proteins and are of relevance for applications such as ssRNA phage-based vaccine design. PubMed: 32917600DOI: 10.1126/sciadv.abc0023 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.794 Å) |
Structure validation
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