3jb2: Difference between revisions

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 <SX load='3jb2' size='340' side='right' viewer='molstar' caption='[[3jb2]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3jb2]] 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=3JB2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3JB2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3jb2]] 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=3JB2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JB2 FirstGlance]. <br>
-</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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</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]] 3.1&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[http://proteopedia.org/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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3jb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jb2 OCA], [https://pdbe.org/3jb2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jb2 RCSB], [https://www.ebi.ac.uk/pdbsum/3jb2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jb2 ProSAT]</span></td></tr>
 </table>
 == 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;">
-== 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>
+==See Also==
+*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, 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__
 </SX>
 [[Category: Bombyx mori cypovirus 1]]
 [[Category: Large Structures]]
-[[Category: Jiang, J S]]
+[[Category: Jiang JS]]
-[[Category: Sun, J C]]
+[[Category: Sun JC]]
-[[Category: Yu, X K]]
+[[Category: Yu XK]]
-[[Category: Zhou, Z H]]
+[[Category: Zhou ZH]]
-[[Category: Conformational change]]
-[[Category: Histidine-mediated guanylyl transfer]]
-[[Category: Regulation of transcription]]
-[[Category: Viral atpase]]
-[[Category: Virus]]