8Q3K
The open state of the ASFV apo-RNA polymerase
Summary for 8Q3K
| Entry DOI | 10.2210/pdb8q3k/pdb |
| Related | 8Q3B |
| EMDB information | 18120 18129 |
| Descriptor | DNA-directed RNA polymerase RPB1 homolog, MAGNESIUM ION, DNA-directed RNA polymerase RPB2 homolog, ... (10 entities in total) |
| Functional Keywords | rna polymerase, asfv, transcription, eukaryotic virus |
| Biological source | African swine fever virus BA71V More |
| Total number of polymer chains | 8 |
| Total formula weight | 445943.11 |
| Authors | Pilotto, S.,Sykora, M.,Cackett, G.,Werner, F. (deposition date: 2023-08-04, release date: 2024-02-14, Last modification date: 2024-03-06) |
| Primary citation | Pilotto, S.,Sykora, M.,Cackett, G.,Dulson, C.,Werner, F. Structure of the recombinant RNA polymerase from African Swine Fever Virus. Nat Commun, 15:1606-1606, 2024 Cited by PubMed Abstract: African Swine Fever Virus is a Nucleo-Cytoplasmic Large DNA Virus that causes an incurable haemorrhagic fever in pigs with a high impact on global food security. ASFV replicates in the cytoplasm of the infected cell and encodes its own transcription machinery that is independent of cellular factors, however, not much is known about how this system works at a molecular level. Here, we present methods to produce recombinant ASFV RNA polymerase, functional assays to screen for inhibitors, and high-resolution cryo-electron microscopy structures of the ASFV RNAP in different conformational states. The ASFV RNAP bears a striking resemblance to RNAPII with bona fide homologues of nine of its twelve subunits. Key differences include the fusion of the ASFV assembly platform subunits RPB3 and RPB11, and an unusual C-terminal domain of the stalk subunit vRPB7 that is related to the eukaryotic mRNA cap 2´-O-methyltransferase 1. Despite the high degree of structural conservation with cellular RNA polymerases, the ASFV RNAP is resistant to the inhibitors rifampicin and alpha-amanitin. The cryo-EM structures and fully recombinant RNAP system together provide an important tool for the design, development, and screening of antiviral drugs in a low biosafety containment environment. PubMed: 38383525DOI: 10.1038/s41467-024-45842-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.92 Å) |
Structure validation
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