3jay

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3jay]] 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=3JAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JAY FirstGlance]. <br>
<table><tr><td colspan='2'>[[3jay]] 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=3JAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JAY FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3jaz|3jaz]], [[3jb0|3jb0]], [[3jb1|3jb1]], [[3jb2|3jb2]], [[3jb3|3jb3]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3jay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jay OCA], [https://pdbe.org/3jay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jay RCSB], [https://www.ebi.ac.uk/pdbsum/3jay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jay 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=3jay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jay OCA], [https://pdbe.org/3jay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jay RCSB], [https://www.ebi.ac.uk/pdbsum/3jay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jay ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://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.
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[https://www.uniprot.org/uniprot/Q914N6_CPVBM Q914N6_CPVBM]
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<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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3jay" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</SX>
</SX>
[[Category: Bombyx mori cypovirus 1]]
[[Category: Bombyx mori cypovirus 1]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Jiang, J S]]
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[[Category: Jiang JS]]
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[[Category: Sun, J C]]
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[[Category: Sun JC]]
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[[Category: Yu, X K]]
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[[Category: Yu XK]]
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[[Category: Zhou, Z H]]
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[[Category: Zhou ZH]]
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[[Category: Conformational change]]
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[[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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Current revision

Atomic model of transcribing cytoplasmic polyhedrosis virus

3jay, resolution 3.00Å

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OCA

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