7S0T

Structure of DNA polymerase zeta with mismatched DNA

Summary for 7S0T

• Entry DOI: 10.2210/pdb7s0t/pdb
• EMDB information: 24793
• Descriptor: DNA polymerase zeta catalytic subunit, DNA polymerase zeta processivity subunit, DNA polymerase delta small subunit, ... (9 entities in total)
• Functional Keywords: dna repair, dna replication, translesion dna synthesis, dna polymerase, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Total number of polymer chains: 7
• Total formula weight: 350341.68

Authors

Malik, R.,Ubarretxena, I.B.,Aggarwal, A.K. (deposition date: 2021-08-31, release date: 2022-03-09, Last modification date: 2024-06-05)

Primary citation

Malik, R.,Johnson, R.E.,Prakash, L.,Prakash, S.,Ubarretxena-Belandia, I.,Aggarwal, A.K.
Cryo-EM structure of translesion DNA synthesis polymerase zeta with a base pair mismatch.
Nat Commun, 13:1050-1050, 2022

PubMed Abstract: The B-family multi-subunit DNA polymerase ζ (Polζ) is important for translesion DNA synthesis (TLS) during replication, due to its ability to extend synthesis past nucleotides opposite DNA lesions and mismatched base pairs. We present a cryo-EM structure of Saccharomyces cerevisiae Polζ with an A:C mismatch at the primer terminus. The structure shows how the Polζ active site responds to the mismatched duplex DNA distortion, including the loosening of key protein-DNA interactions and a fingers domain in an "open" conformation, while the incoming dCTP is still able to bind for the extension reaction. The structure of the mismatched DNA-Polζ ternary complex reveals insights into mechanisms that either stall or favor continued DNA synthesis in eukaryotes.

PubMed: 35217661
DOI: 10.1038/s41467-022-28644-7

Experimental method

ELECTRON MICROSCOPY (3.05 Å)