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8KA3

Arabidopsis AP endonuclease ARP complex with 22bp THF-containing DNA

Summary for 8KA3
Entry DOI10.2210/pdb8ka3/pdb
DescriptorDNA-(apurinic or apyrimidinic site) endonuclease, chloroplastic, DNA (43-MER), NICKEL (II) ION, ... (5 entities in total)
Functional Keywordsap, abasic site, endonuclease, arabidopsis, hydrolase/dna, hydrolase-dna complex
Biological sourceArabidopsis thaliana (Mouse-ear cress)
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Total number of polymer chains4
Total formula weight73754.46
Authors
Guo, W.T.,Wu, B.X. (deposition date: 2023-08-02, release date: 2024-02-21, Last modification date: 2024-06-19)
Primary citationGuo, W.,Wu, W.,Wen, Y.,Gao, Y.,Zhuang, S.,Meng, C.,Chen, H.,Zhao, Z.,Hu, K.,Wu, B.
Structural insights into the catalytic mechanism of the AP endonuclease AtARP.
Structure, 32:780-794.e5, 2024
Cited by
PubMed Abstract: Base excision repair (BER) is a critical genome defense pathway that copes with a broad range of DNA lesions induced by endogenous or exogenous genotoxic agents. AP endonucleases in the BER pathway are responsible for removing the damaged bases and nicking the abasic sites. In plants, the BER pathway plays a critical role in the active demethylation of 5-methylcytosine (5mC) DNA modification. Here, we have determined the crystal structures of Arabidopsis AP endonuclease AtARP in complex with the double-stranded DNA containing tetrahydrofuran (THF) that mimics the abasic site. We identified the critical residues in AtARP for binding and removing the abasic site and the unique residues for interacting with the orphan base. Additionally, we investigated the differences among the three plant AP endonucleases and evaluated the general DNA repair capacity of AtARP in a mammalian cell line. Our studies provide further mechanistic insights into the BER pathway in plants.
PubMed: 38503293
DOI: 10.1016/j.str.2024.02.014
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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