8wh6: Difference between revisions
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==MPOX E5 hexamer ADP and ssDNA bound and clear primase domain conformation== | |||
<StructureSection load='8wh6' size='340' side='right'caption='[[8wh6]], [[Resolution|resolution]] 3.27Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8wh6]] 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=8WH6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8WH6 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]] 3.27Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=8wh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8wh6 OCA], [https://pdbe.org/8wh6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8wh6 RCSB], [https://www.ebi.ac.uk/pdbsum/8wh6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8wh6 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: Dong | <div class="pdbe-citations 8wh6" style="background-color:#fffaf0;"></div> | ||
[[Category: Zhang | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Monkeypox virus]] | |||
[[Category: Spodoptera frugiperda]] | |||
[[Category: Dong C]] | |||
[[Category: Zhang Z]] | |||
Latest revision as of 08:11, 25 September 2024
MPOX E5 hexamer ADP and ssDNA bound and clear primase domain conformationMPOX E5 hexamer ADP and ssDNA bound and clear primase domain 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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