6R0F
Getah virus macro domain in complex with ADPr, pose 1
6R0F の概要
| エントリーDOI | 10.2210/pdb6r0f/pdb |
| 分子名称 | Non-structural polyprotein, [(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL [HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE (3 entities in total) |
| 機能のキーワード | macro domain, getah virus, viral protein |
| 由来する生物種 | Getah virus (GETV) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 37359.66 |
| 構造登録者 | Sulzenbacher, G.,Ferreira Ramos, A.S.,Coutard, B. (登録日: 2019-03-12, 公開日: 2020-04-01, 最終更新日: 2024-01-24) |
| 主引用文献 | Ferreira-Ramos, A.S.,Sulzenbacher, G.,Canard, B.,Coutard, B. Snapshots of ADP-ribose bound to Getah virus macro domain reveal an intriguing choreography. Sci Rep, 10:14422-14422, 2020 Cited by PubMed Abstract: Alphaviruses are (re-)emerging arboviruses of public health concern. The nsP3 gene product is one of the key players during viral replication. NsP3 comprises three domains: a macro domain, a zinc-binding domain and a hypervariable region. The macro domain is essential at both early and late stages of the replication cycle through ADP-ribose (ADPr) binding and de-ADP-ribosylation of host proteins. However, both its specific role and the precise molecular mechanism of de-ADP-ribosylation across specific viral families remains to be elucidated. Here we investigate by X-ray crystallography the mechanism of ADPr reactivity in the active site of Getah virus macro domain, which displays a peculiar substitution of one of the conserved residues in the catalytic loop. ADPr adopts distinct poses including a covalent bond between the C''1 of the ADPr and a conserved Togaviridae-specific cysteine. These different poses observed for ADPr may represent snapshots of the de-ADP-ribosylation mechanism, highlighting residues to be further characterised. PubMed: 32879358DOI: 10.1038/s41598-020-70870-w 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.05 Å) |
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