6YU8
RNA Methyltransferase of Sudan Ebola Virus
Summary for 6YU8
| Entry DOI | 10.2210/pdb6yu8/pdb |
| Descriptor | Methyltransferase domain of the L protein, VHH antiboby, GLYCEROL, ... (8 entities in total) |
| Functional Keywords | rna methyltransferase, virus, ebola, l protein, transferase |
| Biological source | Sudan virus - Boniface, Sudan,1976 More |
| Total number of polymer chains | 2 |
| Total formula weight | 50994.05 |
| Authors | Ferron, F.,Valle, C.,Zamboni, V.,Canard, B.,Decroly, E. (deposition date: 2020-04-25, release date: 2021-02-17, Last modification date: 2024-11-06) |
| Primary citation | Valle, C.,Martin, B.,Ferron, F.,Roig-Zamboni, V.,Desmyter, A.,Debart, F.,Vasseur, J.J.,Canard, B.,Coutard, B.,Decroly, E. First insights into the structural features of Ebola virus methyltransferase activities. Nucleic Acids Res., 49:1737-1748, 2021 Cited by PubMed Abstract: The Ebola virus is a deadly human pathogen responsible for several outbreaks in Africa. Its genome encodes the 'large' L protein, an essential enzyme that has polymerase, capping and methyltransferase activities. The methyltransferase activity leads to RNA co-transcriptional modifications at the N7 position of the cap structure and at the 2'-O position of the first transcribed nucleotide. Unlike other Mononegavirales viruses, the Ebola virus methyltransferase also catalyses 2'-O-methylation of adenosines located within the RNA sequences. Herein, we report the crystal structure at 1.8 Å resolution of the Ebola virus methyltransferase domain bound to a fragment of a camelid single-chain antibody. We identified structural determinants and key amino acids specifically involved in the internal adenosine-2'-O-methylation from cap-related methylations. These results provide the first high resolution structure of an ebolavirus L protein domain, and the framework to investigate the effects of epitranscriptomic modifications and to design possible antiviral drugs against the Filoviridae family. PubMed: 33503246DOI: 10.1093/nar/gkaa1276 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.841 Å) |
Structure validation
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