8wh0: Difference between revisions
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==MPOX E5 hexamer ssDNA and AMP-PNP bound conformation== | |||
<StructureSection load='8wh0' size='340' side='right'caption='[[8wh0]], [[Resolution|resolution]] 2.51Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8wh0]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Monkeypox_virus Monkeypox virus] and [https://en.wikipedia.org/wiki/Spodoptera_frugiperda Spodoptera frugiperda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8WH0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8WH0 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.51Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=8wh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8wh0 OCA], [https://pdbe.org/8wh0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8wh0 RCSB], [https://www.ebi.ac.uk/pdbsum/8wh0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8wh0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5IXS3_MONPV Q5IXS3_MONPV] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
An outbreak of mpox virus in May 2022 has spread over 110 nonpandemic regions in the world, posing a great threat to global health. Mpox virus E5, a helicase-primase, plays an essential role in DNA replication, but the molecular mechanisms are elusive. Here, we report seven structures of mpox virus E5 in a double hexamer (DH) and six in single hexamer in different conformations, indicating a rotation mechanism for helicase and a coupling action for primase. The DH is formed through the interface of zinc-binding domains, and the central channel density indicates potential double-stranded DNA (dsDNA), which helps to identify dsDNA binding residues Arg(249), Lys(286), Lys(315), and Lys(317). Our work is important not only for understanding poxviral DNA replication but also for the development of novel therapeutics for serious poxviral infections including smallpox virus and mpox virus. | |||
Essential and multifunctional mpox virus E5 helicase-primase in double and single hexamer.,Xu Y, Wu Y, Zhang Y, Gao K, Wu X, Yang Y, Li D, Yang B, Zhang Z, Dong C Sci Adv. 2024 Aug 23;10(34):eadl1150. doi: 10.1126/sciadv.adl1150. Epub 2024 Aug , 21. PMID:39167653<ref>PMID:39167653</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8wh0" style="background-color:#fffaf0;"></div> | ||
[[Category: Dong | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Monkeypox virus]] | |||
[[Category: Spodoptera frugiperda]] | |||
[[Category: Dong C]] | |||
[[Category: Zhang Z]] | |||
Latest revision as of 10:03, 9 October 2024
MPOX E5 hexamer ssDNA and AMP-PNP bound conformationMPOX E5 hexamer ssDNA and AMP-PNP bound conformation
Structural highlights
FunctionPublication Abstract from PubMedAn outbreak of mpox virus in May 2022 has spread over 110 nonpandemic regions in the world, posing a great threat to global health. Mpox virus E5, a helicase-primase, plays an essential role in DNA replication, but the molecular mechanisms are elusive. Here, we report seven structures of mpox virus E5 in a double hexamer (DH) and six in single hexamer in different conformations, indicating a rotation mechanism for helicase and a coupling action for primase. The DH is formed through the interface of zinc-binding domains, and the central channel density indicates potential double-stranded DNA (dsDNA), which helps to identify dsDNA binding residues Arg(249), Lys(286), Lys(315), and Lys(317). Our work is important not only for understanding poxviral DNA replication but also for the development of novel therapeutics for serious poxviral infections including smallpox virus and mpox virus. Essential and multifunctional mpox virus E5 helicase-primase in double and single hexamer.,Xu Y, Wu Y, Zhang Y, Gao K, Wu X, Yang Y, Li D, Yang B, Zhang Z, Dong C Sci Adv. 2024 Aug 23;10(34):eadl1150. doi: 10.1126/sciadv.adl1150. Epub 2024 Aug , 21. PMID:39167653[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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