View source for 5izh


==Lassa virus L protein cap-snatching endonuclease. apo form==
<StructureSection load='5izh' size='340' side='right'caption='[[5izh]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</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>
== Function ==
[https://www.uniprot.org/uniprot/L_LASV L_LASV] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:27304209</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5izh" style="background-color:#fffaf0;"></div>

==See Also==
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Lassa mammarenavirus]]
[[Category: Cusack S]]
[[Category: Reguera J]]