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| ==Atomic model of cytoplasmic polyhedrosis virus with GTP== | | ==Atomic model of cytoplasmic polyhedrosis virus with GTP== |
| <StructureSection load='3jb0' size='340' side='right' caption='[[3jb0]], [[Resolution|resolution]] 2.90Å' scene=''> | | <SX load='3jb0' size='340' side='right' viewer='molstar' caption='[[3jb0]], [[Resolution|resolution]] 2.90Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3jb0]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bombyx_mori_cypovirus_1 Bombyx mori cypovirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JB0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JB0 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3jb0]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombyx_mori_cypovirus_1 Bombyx mori cypovirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JB0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JB0 FirstGlance]. <br> |
| </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></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.9Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3jay|3jay]], [[3jaz|3jaz]], [[3jb1|3jb1]], [[3jb2|3jb2]], [[3jb3|3jb3]]</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></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=3jb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jb0 OCA], [http://pdbe.org/3jb0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jb0 RCSB], [http://www.ebi.ac.uk/pdbsum/3jb0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jb0 ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3jb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jb0 OCA], [https://pdbe.org/3jb0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jb0 RCSB], [https://www.ebi.ac.uk/pdbsum/3jb0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jb0 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. | | [https://www.uniprot.org/uniprot/Q914N6_CPVBM Q914N6_CPVBM] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| 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.
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| 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>
| | ==See Also== |
| | | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 3jb0" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </SX> |
| [[Category: Bombyx mori cypovirus 1]] | | [[Category: Bombyx mori cypovirus 1]] |
| [[Category: Jiang, J S]] | | [[Category: Large Structures]] |
| [[Category: Sun, J C]] | | [[Category: Jiang JS]] |
| [[Category: Yu, X K]] | | [[Category: Sun JC]] |
| [[Category: Zhou, Z H]] | | [[Category: Yu XK]] |
| [[Category: Conformational change]] | | [[Category: Zhou ZH]] |
| [[Category: Histidine-mediated guanylyl transfer]]
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| [[Category: Regulation of transcription]]
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| [[Category: Viral atpase]]
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| [[Category: Virus]]
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