3JB2
Atomic model of cytoplasmic polyhedrosis virus with SAM and GTP
3JB2 の概要
エントリーDOI | 10.2210/pdb3jb2/pdb |
関連するPDBエントリー | 3JAY 3JAZ 3JB0 3JB1 3JB3 |
EMDBエントリー | 6371 6374 6375 6376 6377 6378 |
分子名称 | Structural protein VP3, Capsid protein VP1, Viral structural protein 5, ... (6 entities in total) |
機能のキーワード | viral atpase, histidine-mediated guanylyl transfer, conformational changes, regulation of transcription, virus |
由来する生物種 | Bombyx mori cypovirus 1 (BmCPV) 詳細 |
タンパク質・核酸の鎖数 | 5 |
化学式量合計 | 518947.41 |
構造登録者 | |
主引用文献 | Yu, X.,Jiang, J.,Sun, J.,Zhou, Z.H. A putative ATPase mediates RNA transcription and capping in a dsRNA virus. Elife, 4:e07901-e07901, 2015 Cited by PubMed Abstract: mRNA transcription in dsRNA viruses is a highly regulated process but the mechanism of this regulation is not known. Here, by nucleoside triphosphatase (NTPase) assay and comparisons of six high-resolution (2.9-3.1 Å) cryo-electron microscopy structures of cytoplasmic polyhedrosis virus with bound ligands, we show that the large sub-domain of the guanylyltransferase (GTase) domain of the turret protein (TP) also has an ATP-binding site and is likely an ATPase. S-adenosyl-L-methionine (SAM) acts as a signal and binds the methylase-2 domain of TP to induce conformational change of the viral capsid, which in turn activates the putative ATPase. ATP binding/hydrolysis leads to an enlarged capsid for efficient mRNA synthesis, an open GTase domain for His217-mediated guanylyl transfer, and an open methylase-1 domain for SAM binding and methyl transfer. Taken together, our data support a role of the putative ATPase in mediating the activation of mRNA transcription and capping within the confines of the virus. PubMed: 26240998DOI: 10.7554/eLife.07901 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.1 Å) |
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