3VKW
Crystal Structure of the Superfamily 1 Helicase from Tomato Mosaic Virus
3VKW の概要
| エントリーDOI | 10.2210/pdb3vkw/pdb |
| 分子名称 | Replicase large subunit, SULFATE ION (3 entities in total) |
| 機能のキーワード | alpha/beta domain, helicase, transferase |
| 由来する生物種 | Tomato mosaic virus (ToMV) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 50700.98 |
| 構造登録者 | Nishikiori, M.,Sugiyama, S.,Xiang, H.,Niiyama, M.,Ishibashi, K.,Inoue, T.,Ishikawa, M.,Matsumura, H.,Katoh, E. (登録日: 2011-11-22, 公開日: 2012-07-11, 最終更新日: 2024-03-20) |
| 主引用文献 | Nishikiori, M.,Sugiyama, S.,Xiang, H.,Niiyama, M.,Ishibashi, K.,Inoue, T.,Ishikawa, M.,Matsumura, H.,Katoh, E. Crystal structure of the superfamily 1 helicase from tomato mosaic virus J.Virol., 86:7565-7576, 2012 Cited by PubMed Abstract: The genomes of the Tomato mosaic virus and many other plant and animal positive-strand RNA viruses of agronomic and medical importance encode superfamily 1 helicases. Although helicases play important roles in viral replication, the crystal structures of viral superfamily 1 helicases have not been determined. Here, we report the crystal structure of a fragment (S666 to Q1116) of the replication protein from Tomato mosaic virus. The structure reveals a novel N-terminal domain tightly associated with a helicase core. The helicase core contains two RecA-like α/β domains without any of the accessory domain insertions that are found in other superfamily 1 helicases. The N-terminal domain contains a flexible loop, a long α-helix, and an antiparallel six-stranded β-sheet. On the basis of the structure, we constructed deletion mutants of the S666-to-Q1116 fragment and performed split-ubiquitin-based interaction assays in Saccharomyces cerevisiae with TOM1 and ARL8, host proteins that are essential for tomato mosaic virus RNA replication. The results suggested that both TOM1 and ARL8 interact with the long α-helix in the N-terminal domain and that TOM1 also interacts with the helicase core. Prediction of secondary structures in other viral superfamily 1 helicases and comparison of those structures with the S666-to-Q1116 structure suggested that these helicases have a similar fold. Our results provide a structural basis of viral superfamily 1 helicases. PubMed: 22573863DOI: 10.1128/JVI.00118-12 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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