4ztz: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[4ztz]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=4ZTZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZTZ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DCP:2-DEOXYCYTIDINE-5-TRIPHOSPHATE'>DCP</scene>, <scene name='pdbligand=DOC:2,3-DIDEOXYCYTIDINE-5-MONOPHOSPHATE'>DOC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.442&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DCP:2-DEOXYCYTIDINE-5-TRIPHOSPHATE'>DCP</scene>, <scene name='pdbligand=DOC:2,3-DIDEOXYCYTIDINE-5-MONOPHOSPHATE'>DOC</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=4ztz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ztz OCA], [https://pdbe.org/4ztz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ztz RCSB], [https://www.ebi.ac.uk/pdbsum/4ztz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ztz ProSAT]</span></td></tr>
 </table>
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 == Function ==
 [https://www.uniprot.org/uniprot/DPOG1_HUMAN DPOG1_HUMAN] Involved in the replication of mitochondrial DNA. Associates with mitochondrial DNA.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The human DNA polymerase gamma (Pol gamma) is responsible for DNA replication in mitochondria. Pol gamma is particularly susceptible to inhibition by dideoxynucleoside-based inhibitors designed to fight viral infection. Here, we report crystal structures of the replicating Pol gamma-DNA complex bound to either substrate or zalcitabine, an inhibitor used for HIV reverse transcriptase. The structures reveal that zalcitabine binds to the Pol gamma active site almost identically to the substrate dCTP, providing a structural basis for Pol gamma-mediated drug toxicity. When compared to the apo form, Pol gamma undergoes intra- and inter-subunit conformational changes upon formation of the ternary complex with primer/template DNA and substrate. We also find that the accessory subunit Pol gammaB, which lacks intrinsic enzymatic activity and does not contact the primer/template DNA directly, serves as an allosteric regulator of holoenzyme activities. The structures presented here suggest a mechanism for processivity of the holoenzyme and provide a model for understanding the deleterious effects of Pol gamma mutations in human disease. Crystal structures of the mitochondrial DNA polymerase, Pol gamma, in complex with substrate or antiviral inhibitor zalcitabine provide a basis for understanding Pol gamma-mediated drug toxicity.
-Structural basis for processivity and antiviral drug toxicity in human mitochondrial DNA replicase.,Szymanski MR, Kuznetsov VB, Shumate C, Meng Q, Lee YS, Patel G, Patel S, Yin YW EMBO J. 2015 Jul 14;34(14):1959-70. doi: 10.15252/embj.201591520. Epub 2015 Jun, 8. PMID:26056153<ref>PMID:26056153</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4ztz" style="background-color:#fffaf0;"></div>
 ==See Also==