8yge
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==pP1192R-DNA-m-AMSA complex DNA binding/cleavage domain== | |
| + | <StructureSection load='8yge' size='340' side='right'caption='[[8yge]], [[Resolution|resolution]] 2.76Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8yge]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/African_swine_fever_virus_pig/Kenya/KEN-50/1950 African swine fever virus pig/Kenya/KEN-50/1950]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8YGE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8YGE 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]] 2.76Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASW:N-[4-(ACRIDIN-9-YLAMINO)-3-METHOXYPHENYL]METHANESULFONAMIDE'>ASW</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=8yge FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8yge OCA], [https://pdbe.org/8yge PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8yge RCSB], [https://www.ebi.ac.uk/pdbsum/8yge PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8yge ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A0C5B080_ASF A0A0C5B080_ASF] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The African swine fever virus (ASFV) type II topoisomerase (Topo II), pP1192R, is the only known Topo II expressed by mammalian viruses and is essential for ASFV replication in the host cytoplasm. Herein, we report the structures of pP1192R in various enzymatic stages using both X-ray crystallography and single-particle cryo-electron microscopy. Our data structurally define the pP1192R-modulated DNA topology changes. By presenting the A2+-like metal ion at the pre-cleavage site, the pP1192R-DNA-m-AMSA complex structure provides support for the classical two-metal mechanism in Topo II-mediated DNA cleavage and a better explanation for nucleophile formation. The unique inhibitor selectivity of pP1192R and the difunctional mechanism of pP1192R inhibition by m-AMSA highlight the specificity of viral Topo II in the poison binding site. Altogether, this study provides the information applicable to the development of a pP1192R-targeting anti-ASFV strategy. | ||
| - | + | Structural basis for difunctional mechanism of m-AMSA against African swine fever virus pP1192R.,Liu R, Sun J, Li LF, Cheng Y, Li M, Fu L, Li S, Peng G, Wang Y, Liu S, Qu X, Ran J, Li X, Pang E, Qiu HJ, Wang Y, Qi J, Wang H, Gao GF Nucleic Acids Res. 2024 Aug 21:gkae703. doi: 10.1093/nar/gkae703. PMID:39166497<ref>PMID:39166497</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8yge" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: African swine fever virus pig/Kenya/KEN-50/1950]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Liu RL]] | ||
| + | [[Category: Sun JQ]] | ||
Current revision
pP1192R-DNA-m-AMSA complex DNA binding/cleavage domain
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