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| <StructureSection load='7eei' size='340' side='right'caption='[[7eei]], [[Resolution|resolution]] 3.60Å' scene=''> | | <StructureSection load='7eei' size='340' side='right'caption='[[7eei]], [[Resolution|resolution]] 3.60Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[7eei]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EEI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EEI FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EEI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EEI FirstGlance]. <br> |
| </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] </span></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]] 3.6Å</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=7eei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eei OCA], [https://pdbe.org/7eei PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eei RCSB], [https://www.ebi.ac.uk/pdbsum/7eei PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eei 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=7eei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eei OCA], [https://pdbe.org/7eei PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eei RCSB], [https://www.ebi.ac.uk/pdbsum/7eei PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eei ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Rift Valley fever virus (RVFV) belongs to the order Bunyavirales and is the type species of genus Phlebovirus, which accounts for over 50% of family Phenuiviridae species. RVFV is mosquito-borne and causes severe diseases in both humans and livestock, and consists of three segments (S, M, L) in the genome. The L segment encodes an RNA-dependent RNA polymerase (RdRp, L protein) that is responsible for facilitating the replication and transcription of the virus. It is essential for the virus and has multiple drug targets. Here, we established an expression system and purification procedures for full-length L protein, which is composed of an endonuclease domain, RdRp domain, and cap-binding domain. A cryo-EM L protein structure was reported at 3.6 A resolution. In this first L protein structure of genus Phlebovirus, the priming loop of RVFV L protein is distinctly different from those of other L proteins and undergoes large movements related to its replication role. Structural and biochemical analyses indicate that a single template can induce initiation of RNA synthesis, which is notably enhanced by 5' viral RNA. These findings help advance our understanding of the mechanism of RNA synthesis and provide an important basis for developing antiviral inhibitors. Importance The zoonosis RVF virus (RVFV) is one of the most serious arbovirus threats to both human and animal health. RNA-dependent RNA polymerase (RdRp) is a multifunctional enzyme catalyzing genome replication as well as viral transcription, so the RdRp is essential for studying the virus and has multiple drug targets. In our study, we report the structure of RVFV L protein at 3.6 A resolution by cryo-EM. This is the first L protein structure of genus Phlebovirus. Strikingly, a single template can initiate RNA replication. The structure and assays provide a comprehensive and in-depth understanding of the catalytic and substrate recognition mechanism of RdRp.
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| Structure of Rift Valley fever virus RNA-dependent RNA polymerase.,Wang X, Hu C, Ye W, Wang J, Dong X, Xu J, Li X, Zhang M, Lu H, Zhang F, Wu W, Dai S, Wang HW, Chen Z J Virol. 2021 Nov 17:JVI0171321. doi: 10.1128/JVI.01713-21. PMID:34787453<ref>PMID:34787453</ref>
| | ==See Also== |
| | | *[[RNA polymerase 3D structures|RNA polymerase 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 7eei" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: RNA-directed RNA polymerase]]
| | [[Category: Hu CX]] |
| [[Category: Hu, C X]] | | [[Category: Wang X]] |
| [[Category: Wang, X]] | |
| [[Category: Complex]]
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| [[Category: Polymerase]]
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| [[Category: Replicate]]
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| [[Category: Viral protein]]
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