6V93
Structure of DNA Polymerase Zeta/DNA/dNTP Ternary Complex
Summary for 6V93
Entry DOI | 10.2210/pdb6v93/pdb |
EMDB information | 21115 |
Descriptor | DNA polymerase zeta catalytic subunit, DNA polymerase zeta processivity subunit, DNA polymerase delta small subunit, ... (9 entities in total) |
Functional Keywords | dna replication, dna repair, translesion dna synthesis, dna polymerase, dna binding protein |
Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
Total number of polymer chains | 7 |
Total formula weight | 350413.75 |
Authors | Malik, R.,Kopylov, M.,Jain, R.,Ubarrextena-Belandia, I.,Aggarwal, A.K. (deposition date: 2019-12-13, release date: 2020-08-19, Last modification date: 2024-03-06) |
Primary citation | Malik, R.,Kopylov, M.,Gomez-Llorente, Y.,Jain, R.,Johnson, R.E.,Prakash, L.,Prakash, S.,Ubarretxena-Belandia, I.,Aggarwal, A.K. Structure and mechanism of B-family DNA polymerase zeta specialized for translesion DNA synthesis. Nat.Struct.Mol.Biol., 27:913-924, 2020 Cited by PubMed Abstract: DNA polymerase ζ (Polζ) 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 Polζ is unknown. We present cryo-EM structures of the Saccharomyces cerevisiae Polζ holoenzyme in the act of DNA synthesis (3.1 Å) and without DNA (4.1 Å). Polζ 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 Polζ's role in TLS and provide a framework for new cancer therapeutics. PubMed: 32807989DOI: 10.1038/s41594-020-0476-7 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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