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7OM3

Crystal structure of KOD DNA Polymerase in a binary complex with Hypoxanthine containing template

Summary for 7OM3
Entry DOI10.2210/pdb7om3/pdb
DescriptorDNA polymerase,DNA polymerase,DNA polymerase, 21nt Template, Primer, ... (8 entities in total)
Functional Keywordshypoxanthine, binary complex, dna polymerase, replication
Biological sourceThermococcus kodakarensis KOD1
More
Total number of polymer chains3
Total formula weight100661.21
Authors
Betz, K.,Kropp, H.M.,Diederichs, K.,Marx, A. (deposition date: 2021-05-21, release date: 2021-10-13, Last modification date: 2024-11-06)
Primary citationKropp, H.M.,Ludmann, S.,Diederichs, K.,Betz, K.,Marx, A.
Structural Basis for The Recognition of Deaminated Nucleobases by An Archaeal DNA Polymerase.
Chembiochem, 22:3060-3066, 2021
Cited by
PubMed Abstract: With increasing temperature, nucleobases in DNA become increasingly damaged by hydrolysis of exocyclic amines. The most prominent damage includes the conversion of cytosine to uracil and adenine to hypoxanthine. These damages are mutagenic and put the integrity of the genome at risk if not repaired appropriately. Several archaea live at elevated temperatures and thus, are exposed to a higher risk of deamination. Earlier studies have shown that DNA polymerases of archaea have the property of sensing deaminated nucleobases in the DNA template and thereby stalling the DNA synthesis during DNA replication providing another layer of DNA damage recognition and repair. However, the structural basis of uracil and hypoxanthine sensing by archaeal B-family DNA polymerases is sparse. Here we report on three new crystal structures of the archaeal B-family DNA polymerase from Thermococcus kodakarensis (KOD) DNA polymerase in complex with primer and template strands that have extended single stranded DNA template 5'-overhangs. These overhangs contain either the canonical nucleobases as well as uracil or hypoxanthine, respectively, and provide unprecedented structural insights into their recognition by archaeal B-family DNA polymerases.
PubMed: 34486208
DOI: 10.1002/cbic.202100306
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.92 Å)
Structure validation

245663

数据于2025-12-03公开中

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