8Q3K
The open state of the ASFV apo-RNA polymerase
8Q3K の概要
| エントリーDOI | 10.2210/pdb8q3k/pdb |
| 関連するPDBエントリー | 8Q3B |
| EMDBエントリー | 18120 18129 |
| 分子名称 | DNA-directed RNA polymerase RPB1 homolog, MAGNESIUM ION, DNA-directed RNA polymerase RPB2 homolog, ... (10 entities in total) |
| 機能のキーワード | rna polymerase, asfv, transcription, eukaryotic virus |
| 由来する生物種 | African swine fever virus BA71V 詳細 |
| タンパク質・核酸の鎖数 | 8 |
| 化学式量合計 | 445943.11 |
| 構造登録者 | |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (2.92 Å) |
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