View source for 8apm


==Symmetric hexamer of vaccinia virus DNA helicase D5==
<StructureSection load='8apm' size='340' side='right'caption='[[8apm]], [[Resolution|resolution]] 6.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8apm]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Vaccinia_virus_Copenhagen Vaccinia virus Copenhagen] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8APM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8APM 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]] 6.6&#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=8apm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8apm OCA], [https://pdbe.org/8apm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8apm RCSB], [https://www.ebi.ac.uk/pdbsum/8apm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8apm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D5_VACCC D5_VACCC] Primase which may have roles in initiation of DNA replication or lagging-strand synthesis.
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== Publication Abstract from PubMed ==
Poxviruses are large DNA viruses with a linear double-stranded DNA genome circularized at the extremities. The helicase-primase D5, composed of six identical 90 kDa subunits, is required for DNA replication. D5 consists of a primase fragment flexibly attached to the hexameric C-terminal polypeptide (res. 323-785) with confirmed nucleotide hydrolase and DNA-binding activity but an elusive helicase activity. We determined its structure by single-particle cryo-electron microscopy. It displays an AAA+ helicase core flanked by N- and C-terminal domains. Model building was greatly helped by the predicted structure of D5 using AlphaFold2. The 3.9 A structure of the N-terminal domain forms a well-defined tight ring while the resolution decreases towards the C-terminus, still allowing the fit of the predicted structure. The N-terminal domain is partially present in papillomavirus E1 and polyomavirus LTA helicases, as well as in a bacteriophage NrS-1 helicase domain, which is also closely related to the AAA+ helicase domain of D5. Using the Pfam domain database, a D5_N domain followed by DUF5906 and Pox_D5 domains could be assigned to the cryo-EM structure, providing the first 3D structures for D5_N and Pox_D5 domains. The same domain organization has been identified in a family of putative helicases from large DNA viruses, bacteriophages, and selfish DNA elements.

The Vaccinia Virus DNA Helicase Structure from Combined Single-Particle Cryo-Electron Microscopy and AlphaFold2 Prediction.,Hutin S, Ling WL, Tarbouriech N, Schoehn G, Grimm C, Fischer U, Burmeister WP Viruses. 2022 Oct 7;14(10). pii: v14102206. doi: 10.3390/v14102206. PMID:36298761<ref>PMID:36298761</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 8apm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Vaccinia virus Copenhagen]]
[[Category: Burmeister WP]]
[[Category: Grimm C]]
[[Category: Hutin S]]
[[Category: Ling WL]]
[[Category: Schoehn G]]