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5i62

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==Crystal structure of the insertion loop deletion mutant of the RNA-dependent RNA polymerase of a human picorbirnavirus==
==Crystal structure of the insertion loop deletion mutant of the RNA-dependent RNA polymerase of a human picorbirnavirus==
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<StructureSection load='5i62' size='340' side='right' caption='[[5i62]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='5i62' size='340' side='right'caption='[[5i62]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5i62]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I62 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5I62 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5i62]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_picobirnavirus_strain_Hy005102 Human picobirnavirus strain Hy005102]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I62 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5I62 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5i61|5i61]]</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">X-ray diffraction, [[Resolution|Resolution]] 2.001&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] </span></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=5i62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i62 OCA], [https://pdbe.org/5i62 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5i62 RCSB], [https://www.ebi.ac.uk/pdbsum/5i62 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5i62 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5i62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i62 OCA], [http://pdbe.org/5i62 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i62 RCSB], [http://www.ebi.ac.uk/pdbsum/5i62 PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/RDRP_HPBVH RDRP_HPBVH]] RNA-directed RNA polymerase that is involved in both transcription and genome replication.
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[https://www.uniprot.org/uniprot/RDRP_HPBVH RDRP_HPBVH] RNA-directed RNA polymerase that is involved in both transcription and genome replication.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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During the replication cycle of double-stranded (ds) RNA viruses, the viral RNA-dependent RNA polymerase (RdRP) replicates and transcribes the viral genome from within the viral capsid. How the RdRP molecules are packaged within the virion and how they function within the confines of an intact capsid are intriguing questions with answers that most likely vary across the different dsRNA virus families. In this study, we have determined a 2.4 A resolution structure of an RdRP from the human picobirnavirus (hPBV). In addition to the conserved polymerase fold, the hPBV RdRP possesses a highly flexible 24 amino acid loop structure located near the C-terminus of the protein that is inserted into its active site. In vitro RNA polymerization assays and site-directed mutagenesis showed that: (1) the hPBV RdRP is fully active using both ssRNA and dsRNA templates; (2) the insertion loop likely functions as an assembly platform for the priming nucleotide to allow de novo initiation; (3) RNA transcription by the hPBV RdRP proceeds in a semi-conservative manner; and (4) the preference of virus-specific RNA during transcription is dictated by the lower melting temperature associated with the terminal sequences. Co-expression of the hPBV RdRP and the capsid protein (CP) indicated that, under the conditions used, the RdRP could not be incorporated into the recombinant capsids in the absence of the viral genome. Additionally, the hPBV RdRP exhibited higher affinity towards the conserved 5'-terminal sequence of the viral RNA, suggesting that the RdRP molecules may be encapsidated through their specific binding to the viral RNAs during assembly.
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Initiation of RNA Polymerization and Polymerase Encapsidation by a Small dsRNA Virus.,Collier AM, Lyytinen OL, Guo YR, Toh Y, Poranen MM, Tao YJ PLoS Pathog. 2016 Apr 14;12(4):e1005523. doi: 10.1371/journal.ppat.1005523., eCollection 2016 Apr. PMID:27078841<ref>PMID:27078841</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 5i62" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: RNA-directed RNA polymerase]]
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[[Category: Human picobirnavirus strain Hy005102]]
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[[Category: Collier, A M]]
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[[Category: Large Structures]]
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[[Category: Guo, Y R]]
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[[Category: Collier AM]]
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[[Category: Tao, Y J]]
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[[Category: Guo YR]]
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[[Category: Dsrna]]
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[[Category: Tao YJ]]
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[[Category: Insertion loop]]
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[[Category: Replication]]
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[[Category: Transcription]]
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[[Category: Viral protein]]
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Current revision

Crystal structure of the insertion loop deletion mutant of the RNA-dependent RNA polymerase of a human picorbirnavirus

PDB ID 5i62

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