Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	A putative ATPase mediates RNA transcription and capping in a dsRNA virus.
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	6371 3jaz EMDB-6371: A putative ATPase mediates RNA transcription and capping in a dsRNA virus PDB-3jaz: Atomic model of cytoplasmic polyhedrosis virus with ATP Method: EM (single particle) / Resolution: 3.1 Å 6374 3jb0 EMDB-6374: A putative ATPase mediates RNA transcription and capping in a dsRNA virus PDB-3jb0: Atomic model of cytoplasmic polyhedrosis virus with GTP Method: EM (single particle) / Resolution: 2.9 Å 6375 3jb1 EMDB-6375: A putative ATPase mediates RNA transcription and capping in a dsRNA virus PDB-3jb1: Atomic model of cytoplasmic polyhedrosis virus with SAM Method: EM (single particle) / Resolution: 3.1 Å 6376 3jb2 EMDB-6376: A putative ATPase mediates RNA transcription and capping in a dsRNA virus PDB-3jb2: Atomic model of cytoplasmic polyhedrosis virus with SAM and GTP Method: EM (single particle) / Resolution: 3.1 Å 6377 3jb3 EMDB-6377: A putative ATPase mediates RNA transcription and capping in a dsRNA virus PDB-3jb3: Atomic model of cytoplasmic polyhedrosis virus with SAM, GTP and ATP Method: EM (single particle) / Resolution: 3.1 Å 6378 3jay EMDB-6378: A putative ATPase mediates RNA transcription and capping in a dsRNA virus PDB-3jay: Atomic model of transcribing cytoplasmic polyhedrosis virus Method: EM (single particle) / Resolution: 3.0 Å
Chemicals	ChemComp-SAM: S-ADENOSYLMETHIONINE / S-Adenosyl methionine ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM / Adenosine triphosphate ChemComp-GTP: GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying moleculeYM / Guanosine triphosphate ChemComp-MG: Unknown entry
Source	bombyx mori cypovirus 1
Keywords	VIRUS / viral ATPase / histidine-mediated guanylyl transfer / conformational changes / regulation of transcription