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7M0E

Pre-catalytic synaptic complex of DNA Polymerase Lambda with gapped DSB substrate and incoming dUMPNPP

Summary for 7M0E
Entry DOI10.2210/pdb7m0e/pdb
DescriptorDNA polymerase lambda, DNA (5'-D(*CP*GP*GP*CP*AP*GP*C)-3'), DNA (5'-D(*CP*AP*GP*TP*GP*C)-3'), ... (10 entities in total)
Functional Keywordsnonhomologous end-joining, base excision repair, transferase
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains16
Total formula weight177797.09
Authors
Kaminski, A.M.,Bebenek, K.,Pedersen, L.C.,Kunkel, T.A. (deposition date: 2021-03-10, release date: 2022-03-16, Last modification date: 2023-10-25)
Primary citationKaminski, A.M.,Chiruvella, K.K.,Ramsden, D.A.,Bebenek, K.,Kunkel, T.A.,Pedersen, L.C.
Analysis of diverse double-strand break synapsis with Pol lambda reveals basis for unique substrate specificity in nonhomologous end-joining.
Nat Commun, 13:3806-3806, 2022
Cited by
PubMed Abstract: DNA double-strand breaks (DSBs) threaten genomic stability, since their persistence can lead to loss of critical genetic information, chromosomal translocations or rearrangements, and cell death. DSBs can be repaired through the nonhomologous end-joining pathway (NHEJ), which processes and ligates DNA ends efficiently to prevent or minimize sequence loss. Polymerase λ (Polλ), one of the Family X polymerases, fills sequence gaps of DSB substrates with a strict specificity for a base-paired primer terminus. There is little information regarding Polλ's approach to engaging such substrates. We used in vitro polymerization and cell-based NHEJ assays to explore the contributions of conserved loop regions toward DSB substrate specificity and utilization. In addition, we present multiple crystal structures of Polλ in synapsis with varying biologically relevant DSB end configurations, revealing how key structural features and hydrogen bonding networks work in concert to stabilize these tenuous, potentially cytotoxic DNA lesions during NHEJ.
PubMed: 35778389
DOI: 10.1038/s41467-022-31278-4
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.25 Å)
Structure validation

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