View source for 8ywm


==The structure of ASFV DNA polymerase in editing state==
<StructureSection load='8ywm' size='340' side='right'caption='[[8ywm]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8ywm]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/African_swine_fever_virus African swine fever virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8YWM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8YWM 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]] 3.2&#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=8ywm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ywm OCA], [https://pdbe.org/8ywm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ywm RCSB], [https://www.ebi.ac.uk/pdbsum/8ywm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ywm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A2X0SE14_ASF A0A2X0SE14_ASF] DNA-directed DNA polymerase involved in viral DNA replication.[ARBA:ARBA00003644]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
African swine fever virus (ASFV) is one of the most important causative agents of animal diseases and can cause highly fatal diseases in swine. ASFV DNA polymerase (DNAPol) is responsible for genome replication and highly conserved in all viral genotypes showing an ideal target for drug development. Here, we systematically determined the structures of ASFV DNAPol in apo, replicating and editing states. Structural analysis revealed that ASFV DNAPol had a classical right-handed structure and showed the highest similarity to the structure of human polymerase delta. Intriguingly, ASFV DNAPol has a much longer fingers subdomain, and the thumb and palm subdomain form a unique interaction that has never been seen. Mutagenesis work revealed that the loss of this unique interaction decreased the enzymatic activity. We also found that the beta-hairpin of ASFV DNAPol is located below the template strand in the editing state, which is different from the editing structures of other known B family DNAPols with the beta-hairpin above the template strand. It suggests that B family DNAPols have evolved two ways to facilitate the dsDNA unwinding during the transition from replicating into editing state. These findings figured out the working mechanism of ASFV DNAPol and will provide a critical structural basis for the development of antiviral drugs.

Cryo-EM structure of DNA polymerase of African swine fever virus.,Kuai L, Sun J, Peng Q, Zhao X, Yuan B, Liu S, Bi Y, Shi Y Nucleic Acids Res. 2024 Sep 23;52(17):10717-10729. doi: 10.1093/nar/gkae739. PMID:39189451<ref>PMID:39189451</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8ywm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: African swine fever virus]]
[[Category: Large Structures]]
[[Category: Kuai L]]
[[Category: Peng Q]]
[[Category: Shi Y]]
[[Category: Sun JQ]]