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-Structure paper
Title | A putative ATPase mediates RNA transcription and capping in a dsRNA virus. |
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Journal, issue, pages | Elife, Vol. 4, Page e07901, Year 2015 |
Publish date | Aug 4, 2015 |
Authors | Xuekui Yu / Jiansen Jiang / Jingchen Sun / Z Hong Zhou / |
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- ...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. |
External links | Elife / PubMed:26240998 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.9 - 3.1 Å |
Structure data | EMDB-6371: A putative ATPase mediates RNA transcription and capping in a dsRNA virus EMDB-6374: A putative ATPase mediates RNA transcription and capping in a dsRNA virus EMDB-6375: A putative ATPase mediates RNA transcription and capping in a dsRNA virus EMDB-6376: A putative ATPase mediates RNA transcription and capping in a dsRNA virus |
Chemicals | ChemComp-SAM: ChemComp-ATP: ChemComp-GTP: ChemComp-MG: |
Source |
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Keywords | VIRUS / viral ATPase / histidine-mediated guanylyl transfer / conformational changes / regulation of transcription |