3jb2: Difference between revisions
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==Atomic model of cytoplasmic polyhedrosis virus with SAM and GTP== | ==Atomic model of cytoplasmic polyhedrosis virus with SAM and GTP== | ||
<StructureSection load='3jb2' size='340' side='right' caption='[[3jb2]], [[Resolution|resolution]] 3.10Å' scene=''> | <StructureSection load='3jb2' size='340' side='right' caption='[[3jb2]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3jay|3jay]], [[3jaz|3jaz]], [[3jb0|3jb0]], [[3jb1|3jb1]], [[3jb3|3jb3]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3jay|3jay]], [[3jaz|3jaz]], [[3jb0|3jb0]], [[3jb1|3jb1]], [[3jb3|3jb3]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3jb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jb2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3jb2 RCSB], [http://www.ebi.ac.uk/pdbsum/3jb2 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3jb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jb2 OCA], [http://pdbe.org/3jb2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jb2 RCSB], [http://www.ebi.ac.uk/pdbsum/3jb2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jb2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/CAPSD_CPVBM CAPSD_CPVBM]] Capsid protein self-assembles to form an icosahedral capsid with a pseudo T=2 symmetry, about 50 nm in diameter, and consisting of 120 capsid proteins. The capsid encapsulates the genomic RNA. | [[http://www.uniprot.org/uniprot/CAPSD_CPVBM CAPSD_CPVBM]] Capsid protein self-assembles to form an icosahedral capsid with a pseudo T=2 symmetry, about 50 nm in diameter, and consisting of 120 capsid proteins. The capsid encapsulates the genomic RNA. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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 A) 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. | |||
A putative ATPase mediates RNA transcription and capping in a dsRNA virus.,Yu X, Jiang J, Sun J, Zhou ZH Elife. 2015 Aug 4;4:e07901. doi: 10.7554/eLife.07901. PMID:26240998<ref>PMID:26240998</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3jb2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 14:11, 2 November 2016
Atomic model of cytoplasmic polyhedrosis virus with SAM and GTPAtomic model of cytoplasmic polyhedrosis virus with SAM and GTP
Structural highlights
Function[CAPSD_CPVBM] Capsid protein self-assembles to form an icosahedral capsid with a pseudo T=2 symmetry, about 50 nm in diameter, and consisting of 120 capsid proteins. The capsid encapsulates the genomic RNA. Publication Abstract from PubMedmRNA 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 A) 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. A putative ATPase mediates RNA transcription and capping in a dsRNA virus.,Yu X, Jiang J, Sun J, Zhou ZH Elife. 2015 Aug 4;4:e07901. doi: 10.7554/eLife.07901. PMID:26240998[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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