6Z8K
La Crosse virus polymerase at elongation mimicking stage
Summary for 6Z8K
| Entry DOI | 10.2210/pdb6z8k/pdb |
| Related | 6Z6G |
| EMDB information | 11093 11095 11107 11118 |
| Descriptor | La Crosse virus 5' vRNA 1-10, La Crosse virus 5' vRNA (9-16), La Crosse virus 3' vRNA (1-16), ... (6 entities in total) |
| Functional Keywords | polymerase, transcription, replication, la crosse virus |
| Biological source | La Crosse orthobunyavirus More |
| Total number of polymer chains | 6 |
| Total formula weight | 285202.72 |
| Authors | Arragain, B.,Effantin, G.,Schoehn, G.,Cusack, S.,Malet, H. (deposition date: 2020-06-02, release date: 2020-07-29, Last modification date: 2024-05-01) |
| Primary citation | Arragain, B.,Effantin, G.,Gerlach, P.,Reguera, J.,Schoehn, G.,Cusack, S.,Malet, H. Pre-initiation and elongation structures of full-length La Crosse virus polymerase reveal functionally important conformational changes. Nat Commun, 11:3590-3590, 2020 Cited by PubMed Abstract: Bunyavirales is an order of segmented negative-strand RNA viruses comprising several life-threatening pathogens against which no effective treatment is currently available. Replication and transcription of the RNA genome constitute essential processes performed by the virally encoded multi-domain RNA-dependent RNA polymerase. Here, we describe the complete high-resolution cryo-EM structure of La Crosse virus polymerase. It reveals the presence of key protruding C-terminal domains, notably the cap-binding domain, which undergoes large movements related to its role in transcription initiation, and a zinc-binding domain that displays a fold not previously observed. We capture the polymerase structure at pre-initiation and elongation states, uncovering the coordinated movement of the priming loop, mid-thumb ring linker and lid domain required for the establishment of a ten-base-pair template-product RNA duplex before strand separation into respective exit tunnels. These structural details and the observed dynamics of key functional elements will be instrumental for structure-based development of polymerase inhibitors. PubMed: 32681014DOI: 10.1038/s41467-020-17349-4 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.02 Å) |
Structure validation
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