6v8p
From Proteopedia
(Difference between revisions)
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<table><tr><td colspan='2'>[[6v8p]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6V8P FirstGlance]. <br> | <table><tr><td colspan='2'>[[6v8p]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6V8P 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]] 4.1Å</td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.1Å</td></tr> | ||
- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=6v8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v8p OCA], [https://pdbe.org/6v8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6v8p RCSB], [https://www.ebi.ac.uk/pdbsum/6v8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6v8p 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=6v8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v8p OCA], [https://pdbe.org/6v8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6v8p RCSB], [https://www.ebi.ac.uk/pdbsum/6v8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6v8p ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/DPOZ_YEAST DPOZ_YEAST] Nonessential DNA polymerase. Required for DNA damage induced mutagenesis. Involved in DNA repair, mitochondrial DNA repair and translesion synthesis. Translesion synthesis in S.cerevisiae may use a specialized DNA polymerase that is not required for other DNA replicative processes. Has a role in the bypass of abasic (AP) sites. Highly inefficient in incorporating nucleotides opposite the AP site, but efficiently extends from nucleotides, particularly an A, inserted opposite the lesion.<ref>PMID:11316789</ref> <ref>PMID:16452144</ref> <ref>PMID:2676986</ref> <ref>PMID:8658138</ref> | [https://www.uniprot.org/uniprot/DPOZ_YEAST DPOZ_YEAST] Nonessential DNA polymerase. Required for DNA damage induced mutagenesis. Involved in DNA repair, mitochondrial DNA repair and translesion synthesis. Translesion synthesis in S.cerevisiae may use a specialized DNA polymerase that is not required for other DNA replicative processes. Has a role in the bypass of abasic (AP) sites. Highly inefficient in incorporating nucleotides opposite the AP site, but efficiently extends from nucleotides, particularly an A, inserted opposite the lesion.<ref>PMID:11316789</ref> <ref>PMID:16452144</ref> <ref>PMID:2676986</ref> <ref>PMID:8658138</ref> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | DNA polymerase zeta (Polzeta) belongs to the same B-family as high-fidelity replicative polymerases, yet is specialized for the extension reaction in translesion DNA synthesis (TLS). Despite its importance in TLS, the structure of Polzeta is unknown. We present cryo-EM structures of the Saccharomyces cerevisiae Polzeta holoenzyme in the act of DNA synthesis (3.1 A) and without DNA (4.1 A). Polzeta displays a pentameric ring-like architecture, with catalytic Rev3, accessory Pol31' Pol32 and two Rev7 subunits forming an uninterrupted daisy chain of protein-protein interactions. We also uncover the features that impose high fidelity during the nucleotide-incorporation step and those that accommodate mismatches and lesions during the extension reaction. Collectively, we decrypt the molecular underpinnings of Polzeta's role in TLS and provide a framework for new cancer therapeutics. | ||
+ | |||
+ | Structure and mechanism of B-family DNA polymerase zeta specialized for translesion DNA synthesis.,Malik R, Kopylov M, Gomez-Llorente Y, Jain R, Johnson RE, Prakash L, Prakash S, Ubarretxena-Belandia I, Aggarwal AK Nat Struct Mol Biol. 2020 Oct;27(10):913-924. doi: 10.1038/s41594-020-0476-7., Epub 2020 Aug 17. PMID:32807989<ref>PMID:32807989</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 6v8p" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== |
Current revision
Structure of DNA Polymerase Zeta (Apo)
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