6k32

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<SX load='6k32' size='340' side='right' viewer='molstar' caption='[[6k32]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<SX load='6k32' size='340' side='right' viewer='molstar' caption='[[6k32]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6k32]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Cpv-1 Cpv-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K32 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6K32 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6k32]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Cypovirus_1 Cypovirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6K32 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=A2M:2-O-METHYLADENOSINE+5-(DIHYDROGEN+PHOSPHATE)'>A2M</scene>, <scene name='pdbligand=DPO:DIPHOSPHATE'>DPO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MG7:7-METHYLGUANOSINE'>MG7</scene>, <scene name='pdbligand=UTP:URIDINE+5-TRIPHOSPHATE'>UTP</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]] 3.2&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=3PO:TRIPHOSPHATE'>3PO</scene></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=3PO:TRIPHOSPHATE'>3PO</scene>, <scene name='pdbligand=A2M:2-O-METHYLADENOSINE+5-(DIHYDROGEN+PHOSPHATE)'>A2M</scene>, <scene name='pdbligand=DPO:DIPHOSPHATE'>DPO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MG7:7-METHYLGUANOSINE'>MG7</scene>, <scene name='pdbligand=UTP:URIDINE+5-TRIPHOSPHATE'>UTP</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VP4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=205895 CPV-1])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6k32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k32 OCA], [https://pdbe.org/6k32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k32 RCSB], [https://www.ebi.ac.uk/pdbsum/6k32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k32 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6k32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k32 OCA], [http://pdbe.org/6k32 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k32 RCSB], [http://www.ebi.ac.uk/pdbsum/6k32 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k32 ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/D0EZK6_CPVBM D0EZK6_CPVBM]
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RNA-dependent RNA polymerases (RdRps) catalyze RNA synthesis of RNA viruses. During initiation of RNA synthesis, the RdRp catalyzes the formation of the first dinucleotide, acting as primer for subsequent processive RNA elongation. Here, we present the structure of the RdRp complexes in the dinucleotide primed state in situ within a transcribing cypovirus under near physiological conditions using cryo-electron microscopy. The 3' end of RNA templates, paired RNA dinucleotide primer, incoming nucleotide, and catalytic divalent cations in the RdRp were resolved at 3.8 A resolution. The end of the RNA template and the dinucleotide is buttressed by the aromatic tyrosine in a loop from the RdRp bracelet domain. Our structure reveals the interactions between the nucleotide substrates and the conserved residues during the RdRp initiation, and the coordinated structural changes preceding the elongation stage. In addition, it provides the direct evidence for existence of the slow step of the dinucleotide primed state in the viral RdRp transcription.
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Structure of RdRps within a transcribing dsRNA virus provides insights into the mechanisms of RNA synthesis.,Li X, Wang L, Wang X, Chen W, Yang T, Song J, Liu H, Cheng L J Mol Biol. 2019 Oct 17. pii: S0022-2836(19)30570-4. doi:, 10.1016/j.jmb.2019.09.015. PMID:31629769<ref>PMID:31629769</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 6k32" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</SX>
</SX>
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[[Category: Cpv-1]]
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[[Category: Cypovirus 1]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Li, X W]]
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[[Category: Li XW]]
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[[Category: Cypovirus]]
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[[Category: Rna-dependent rna polymerase]]
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[[Category: Transcription]]
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[[Category: Viral protein-rna complex]]
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Revision as of 10:40, 27 March 2024

RdRp complex

6k32, resolution 3.20Å

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