View source for 8hwa


==D5 ATP-ADP-Apo-ssDNA IS1==
<StructureSection load='8hwa' size='340' side='right'caption='[[8hwa]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8hwa]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Monkeypox_virus Monkeypox virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HWA 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]] 3.7&#8491;</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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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=8hwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hwa OCA], [https://pdbe.org/8hwa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hwa RCSB], [https://www.ebi.ac.uk/pdbsum/8hwa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hwa ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PG117_MONPV PG117_MONPV] Multifunctional protein required for genome uncoating and replication. Major viral uncoating protein that is required for the release of the viral genome from incoming viral cores containing the viral DNA genome. Possesses an ATPase activity that is required for hexamerization and uncoating.[UniProtKB:P04305]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Mpox pandemic, caused by the Mpox virus (or monkeypox virus, MPXV), has gained global attention. The D5 protein, a putative helicase-primase found in MPXV, plays a vital role in viral replication and genome uncoating. Here we determined multiple cryo-EM structures of full-length hexameric D5 in diverse states. These states were captured during ATP hydrolysis while moving along the single-stranded DNA (ssDNA) track. Through comprehensive structural analysis combined with the helicase activity system, we revealed that when the primase domain is truncated or the interaction between the primase and helicase domains is disrupted, the double-stranded DNA (dsDNA) unwinds into ssDNA, suggesting a critical regulatory role of the primase domain. Two transition states bound with ssDNA substrate during unwinding reveals that two ATP molecules were consumed to drive DNA moving forward two nucleotides. Collectively, our findings shed light on the molecular mechanism that links ATP hydrolysis to the DNA unwinding in poxviruses.

Structural insight into the assembly and working mechanism of helicase-primase D5 from Mpox virus.,Li Y, Zhu J, Guo Y, Yan R Nat Struct Mol Biol. 2024 Jan;31(1):68-81. doi: 10.1038/s41594-023-01142-0. Epub , 2024 Jan 4. PMID:38177671<ref>PMID:38177671</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8hwa" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Monkeypox virus]]
[[Category: Guo YY]]
[[Category: Li YN]]
[[Category: Yan RH]]
[[Category: Zhu J]]