6ljo

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Current revision (10:46, 27 March 2024) (edit) (undo)
 
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<StructureSection load='6ljo' size='340' side='right'caption='[[6ljo]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
<StructureSection load='6ljo' size='340' side='right'caption='[[6ljo]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6ljo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Asf Asf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LJO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LJO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6ljo]] is a 1 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=6LJO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LJO FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">E165R CDS, E165R, ASFV-Georgia_4-154, ASFV_Kyiv_2016_131_00207 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10497 ASF])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.28&#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=6ljo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ljo OCA], [https://pdbe.org/6ljo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ljo RCSB], [https://www.ebi.ac.uk/pdbsum/6ljo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ljo ProSAT]</span></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=6ljo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ljo OCA], [https://pdbe.org/6ljo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ljo RCSB], [https://www.ebi.ac.uk/pdbsum/6ljo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ljo ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/DUTP_ASFB7 DUTP_ASFB7] The viral dUTPase may play a role in lowering the dUTP concentration in natural infections to minimize misincorporation of deoxyuridine into the viral DNA and ensure the fidelity of genome replication.<ref>PMID:10515998</ref>
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African swine fever, caused by the African swine fever virus (ASFV), is among the most significant swine diseases. There are currently no effective treatments against ASFV. ASFV contains a gene encoding a dUTPase (E165R), which is required for viral replication in swine macrophages, making it an attractive target for inhibitor development. However, the full structural details of the ASFV dUTPase and those of the comparable swine enzyme are not available, limiting further insights. Herein, we determine the crystal structures of ASFV dUTPase and swine dUTPase in both their ligand-free and ligand-bound forms. We observe that the swine enzyme employs a classical dUTPase architecture made up of three-subunit active sites, whereas the ASFV enzyme employs a novel two-subunit active site. We then performed a comparative analysis of all dUTPase structures uploaded in PDB, which showed classic and non-classical types were mainly determined by the C-terminal beta-strand orientation, and the difference was mainly related to the four amino acids behind motif IV. Thus, our study not only explains the reason for the structural diversity of dUTPase but also reveals how to predict dUTPase type, which may have implications for the dUTPase family. Finally, we tested two dUTPase inhibitors developed for the Plasmodium falciparum dUTPase against the swine and ASFV enzymes. One of these compounds inhibited the ASFV dUTPase at low micromolar concentrations (Kd =15.6muM) and with some selectivity (~2x) over swine dUTPase. In conclusion, our study expands our understanding of the dUTPase family and may aid in the development of specific ASFV inhibitors.
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Structural comparisons of host and African swine fever virus dUTPases reveal new clues for inhibitor development.,Liang R, Wang G, Zhang D, Ye G, Li M, Shi Y, Shi J, Chen H, Peng G J Biol Chem. 2020 Nov 2. pii: RA120.014005. doi: 10.1074/jbc.RA120.014005. PMID:33139328<ref>PMID:33139328</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6ljo" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Asf]]
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[[Category: African swine fever virus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Liang, R]]
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[[Category: Liang R]]
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[[Category: Peng, G Q]]
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[[Category: Peng GQ]]
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[[Category: Adut]]
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[[Category: Asfv]]
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[[Category: Dutpase]]
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[[Category: Viral protein]]
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Current revision

African swine fever virus dUTPase

PDB ID 6ljo

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