8QHD
Hantaan virus polymerase in hexameric state
8QHD の概要
| エントリーDOI | 10.2210/pdb8qhd/pdb |
| EMDBエントリー | 18408 |
| 分子名称 | RNA-directed RNA polymerase L (1 entity in total) |
| 機能のキーワード | bunyavirus, hantaan virus, polymerase, dimer, viral protein |
| 由来する生物種 | Hantaan virus 76-118 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 1496858.90 |
| 構造登録者 | |
| 主引用文献 | Durieux Trouilleton, Q.,Housset, D.,Tarillon, P.,Arragain, B.,Malet, H. Structural characterization of the oligomerization of full-length Hantaan virus polymerase into symmetric dimers and hexamers. Nat Commun, 15:2256-2256, 2024 Cited by PubMed Abstract: Hantaan virus is a dangerous human pathogen whose segmented negative-stranded RNA genome is replicated and transcribed by a virally-encoded multi-functional polymerase. Here we describe the complete cryo-electron microscopy structure of Hantaan virus polymerase in several oligomeric forms. Apo polymerase protomers can adopt two drastically different conformations, which assemble into two distinct symmetric homodimers, that can themselves gather to form hexamers. Polymerase dimerization induces the stabilization of most polymerase domains, including the C-terminal domain that contributes the most to dimer's interface, along with a lariat region that participates to the polymerase steadying. Binding to viral RNA induces significant conformational changes resulting in symmetric oligomer disruption and polymerase activation, suggesting the possible involvement of apo multimers as protecting systems that would stabilize the otherwise flexible C-terminal domains. Overall, these results provide insights into the multimerization capability of Hantavirus polymerase and may help to define antiviral compounds to counteract these life-threatening viruses. PubMed: 38480734DOI: 10.1038/s41467-024-46601-4 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.6 Å) |
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