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| | <StructureSection load='5izh' size='340' side='right'caption='[[5izh]], [[Resolution|resolution]] 1.85Å' scene=''> | | <StructureSection load='5izh' size='340' side='right'caption='[[5izh]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5izh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lassa_mammarenavirus Lassa mammarenavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IZH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5IZH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5izh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lassa_mammarenavirus Lassa mammarenavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IZH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IZH FirstGlance]. <br> |
| - | </td></tr><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</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=5izh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5izh OCA], [http://pdbe.org/5izh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5izh RCSB], [http://www.ebi.ac.uk/pdbsum/5izh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5izh 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=5izh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5izh OCA], [https://pdbe.org/5izh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5izh RCSB], [https://www.ebi.ac.uk/pdbsum/5izh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5izh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q6GWS6_9VIRU Q6GWS6_9VIRU]] RNA-dependent RNA polymerase which is responsible for replication and transcription of the viral RNA genome. During transcription, synthesizes 4 subgenomic RNAs, and assures their capping by a cap-snatching mechanism, in which cellular capped pre-mRNA are used to generate primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are heterogeneous and not polyadenylated. The replicase function is to direct synthesis of antigenomic and genomic RNA which are encapsidated and non capped. As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated. These processes may be regulated by proteins N and Z in a dose-dependent manner.[PIRNR:PIRNR000836] | + | [https://www.uniprot.org/uniprot/L_LASV L_LASV] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Lassa mammarenavirus]] | | [[Category: Lassa mammarenavirus]] |
| - | [[Category: RNA-directed RNA polymerase]]
| + | [[Category: Cusack S]] |
| - | [[Category: Cusack, S]] | + | [[Category: Reguera J]] |
| - | [[Category: Reguera, J]] | + | |
| - | [[Category: Cap-snatching nuclease lassa transcription]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
L_LASV
Publication Abstract from PubMed
Segmented negative strand RNA viruses of the arena-, bunya- and orthomyxovirus families uniquely carry out viral mRNA transcription by the cap-snatching mechanism. This involves cleavage of host mRNAs close to their capped 5' end by an endonuclease (EN) domain located in the N-terminal region of the viral polymerase. We present the structure of the cap-snatching EN of Hantaan virus, a bunyavirus belonging to hantavirus genus. Hantaan EN has an active site configuration, including a metal co-ordinating histidine, and nuclease activity similar to the previously reported La Crosse virus and Influenza virus ENs (orthobunyavirus and orthomyxovirus respectively), but is more active in cleaving a double stranded RNA substrate. In contrast, Lassa arenavirus EN has only acidic metal co-ordinating residues. We present three high resolution structures of Lassa virus EN with different bound ion configurations and show in comparative biophysical and biochemical experiments with Hantaan, La Crosse and influenza ENs that the isolated Lassa EN is essentially inactive. The results are discussed in the light of EN activation mechanisms revealed by recent structures of full-length influenza virus polymerase.
Comparative Structural and Functional Analysis of Bunyavirus and Arenavirus Cap-Snatching Endonucleases.,Reguera J, Gerlach P, Rosenthal M, Gaudon S, Coscia F, Gunther S, Cusack S PLoS Pathog. 2016 Jun 15;12(6):e1005636. doi: 10.1371/journal.ppat.1005636., eCollection 2016 Jun. PMID:27304209[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Reguera J, Gerlach P, Rosenthal M, Gaudon S, Coscia F, Gunther S, Cusack S. Comparative Structural and Functional Analysis of Bunyavirus and Arenavirus Cap-Snatching Endonucleases. PLoS Pathog. 2016 Jun 15;12(6):e1005636. doi: 10.1371/journal.ppat.1005636., eCollection 2016 Jun. PMID:27304209 doi:http://dx.doi.org/10.1371/journal.ppat.1005636
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