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-Structure paper
| タイトル | Structure of the Newcastle Disease Virus L protein in complex with tetrameric phosphoprotein. |
|---|---|
| ジャーナル・号・ページ | Nat Commun, Vol. 14, Issue 1, Page 1324, Year 2023 |
| 掲載日 | 2023年3月10日 |
著者 | Jingyuan Cong / Xiaoying Feng / Huiling Kang / Wangjun Fu / Lei Wang / Chenlong Wang / Xuemei Li / Yutao Chen / Zihe Rao / ![]() |
| PubMed 要旨 | Newcastle disease virus (NDV) belongs to Paramyxoviridae, which contains lethal human and animal pathogens. NDV RNA genome is replicated and transcribed by a multifunctional 250 kDa RNA-dependent ...Newcastle disease virus (NDV) belongs to Paramyxoviridae, which contains lethal human and animal pathogens. NDV RNA genome is replicated and transcribed by a multifunctional 250 kDa RNA-dependent RNA polymerase (L protein). To date, high-resolution structure of NDV L protein complexed with P protein remains to be elucidated, limiting our understanding of the molecular mechanisms of Paramyxoviridae replication/transcription. Here, we used cryo-EM and enzymatic assays to investigate the structure-function relationship of L-P complex. We found that C-terminal of CD-MTase-CTD module of the atomic-resolution L-P complex conformationally rearranges, and the priming/intrusion loops are likely in RNA elongation conformations different from previous structures. The P protein adopts a unique tetrameric organization and interacts with L protein. Our findings indicate that NDV L-P complex represents elongation state distinct from previous structures. Our work greatly advances the understanding of Paramyxoviridae RNA synthesis, revealing how initiation/elongation alternates, providing clues for identifying therapeutic targets against Paramyxoviridae. |
リンク | Nat Commun / PubMed:36898997 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 3.0 - 3.41 Å |
| 構造データ | EMDB-33986, PDB-7yot: EMDB-33987, PDB-7you: EMDB-33988, PDB-7yov: |
| 由来 |
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キーワード | VIRUS / cryo-EM / L-P complex / Newcastle disease virus |
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avian orthoavulavirus 1 (ウイルス)
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