9JKC
Crystal structure of Aspergillus fumigatus polymycovirus 1 ploymerase (residues 85-763) in its apo state
Summary for 9JKC
| Entry DOI | 10.2210/pdb9jkc/pdb |
| Descriptor | RNA dependent RNA polymerase (2 entities in total) |
| Functional Keywords | rna virus, rna-dependent rna polymerase, viral protein |
| Biological source | Aspergillus fumigatus tetramycovirus 1 |
| Total number of polymer chains | 5 |
| Total formula weight | 384566.17 |
| Authors | |
| Primary citation | Jia, H.,Liu, S.,Rao, G.,Liu, Q.,Wu, J.,Cao, S.,Gong, P. An evolutionarily unique viral RdRP suggests a common dual-function feature of the priming element. Sci Adv, 11:eadv9640-eadv9640, 2025 Cited by PubMed Abstract: Many RNA-dependent RNA polymerases (RdRPs) encoded by RNA viruses use de novo initiation strategy to start RNA synthesis, and they usually contain a priming element (PE) to interact with template RNA and priming nucleoside triphosphate to facilitate initiation. Upon transition to elongation in dengue virus 2 (DENV2) RdRP, PE refolds and contributes to elongation complex stability by interacting with the upstream RNA duplex. However, whether this PE dual-function feature commonly exists in viral RdRPs remains elusive, as PE is highly diverse among the entire RNA virus group. Here, a more complexed PE refolding is observed in RdRP crystal structures of polymycovirus-1 (AfuPmV-1), a polymycovirus evolutionarily connecting positive-strand and double-stranded RNA viruses. Although structural details and enzymology features are very different in transition from initiation to elongation in DENV2 and AfuPmV-1 RdRPs, what is in common is the PE dual-function feature that demonstrates functional conservation beyond sequence and structure. PubMed: 40249801DOI: 10.1126/sciadv.adv9640 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.4 Å) |
Structure validation
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