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-Structure paper
Title | Cryo-EM structure of translesion DNA synthesis polymerase ζ with a base pair mismatch. |
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Journal, issue, pages | Nat Commun, Vol. 13, Issue 1, Page 1050, Year 2022 |
Publish date | Feb 25, 2022 |
Authors | Radhika Malik / Robert E Johnson / Louise Prakash / Satya Prakash / Iban Ubarretxena-Belandia / Aneel K Aggarwal / |
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 ...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. |
External links | Nat Commun / PubMed:35217661 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.05 Å |
Structure data | EMDB-24793, PDB-7s0t: |
Chemicals | ChemComp-SF4: ChemComp-CA: ChemComp-DCP: ChemComp-HOH: |
Source |
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Keywords | DNA BINDING PROTEIN/DNA / DNA repair / DNA replication / translesion DNA synthesis / DNA polymerase / DNA BINDING PROTEIN-DNA complex |