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6V93

Structure of DNA Polymerase Zeta/DNA/dNTP Ternary Complex

Summary for 6V93
Entry DOI10.2210/pdb6v93/pdb
EMDB information21115
DescriptorDNA polymerase zeta catalytic subunit, DNA polymerase zeta processivity subunit, DNA polymerase delta small subunit, ... (9 entities in total)
Functional Keywordsdna replication, dna repair, translesion dna synthesis, dna polymerase, dna binding protein
Biological sourceSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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Total number of polymer chains7
Total formula weight350413.75
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 citationMalik, 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: 32807989
DOI: 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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