ArticleActa crystallographica. Section D, Biological crystallography2013
Structure of human apurinic/apyrimidinic endonuclease 1 with the essential Mg2+ cofactor.
Article in Acta crystallographica. Section D, Biological crystallography, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 41 citations in OpenAlex.
- CHA-mediated split G-quadruplex assembly: a ratiometric AIE strategy for label-free detection of APE1.Analytical and bioanalytical chemistry · 2026Article
- Structural basis for the mechanism and stability of the EEPD1 5' endonuclease.The Journal of biological chemistry · 2026Article
- APE1 coordinates its disordered region and metal cofactors to drive genome surveillance.Nucleic acids research · 2026Article
- Characterization of a Novel Thermostable DNA Lyase Used To Prepare DNA for Next-Generation Sequencing.Chemical research in toxicology · 2023Article
- Characterizing inhibitors of human AP endonuclease 1.PloS one · 2023Article
- Insights into Mechanisms of Damage Recognition and Catalysis by APE1-like Enzymes.International journal of molecular sciences · 2022Article
- Comparative Analysis of Exo- and Endonuclease Activities of APE1-like Enzymes.International journal of molecular sciences · 2022Article
- The Enigma of Substrate Recognition and Catalytic Efficiency of APE1-Like Enzymes.Frontiers in cell and developmental biology · 2021Article
- Mutational and Kinetic Analysis of APE1 Endoribonuclease Activity.Molecular biology · 2021Article
- The Role of Active-Site Plasticity in Damaged-Nucleotide Recognition by Human Apurinic/Apyrimidinic Endonuclease APE1.Molecules (Basel, Switzerland) · 2020Article
- Activity of Human Apurinic/Apyrimidinic Endonuclease APE1 Toward Damaged DNA and Native RNA With Non-canonical Structures.Frontiers in cell and developmental biology · 2020Article
- DNA complexes with human apurinic/apyrimidinic endonuclease 1: structural insights revealed by pulsed dipolar EPR with orthogonal spin labeling.Nucleic acids research · 2019Article
- Substrate specificity of human apurinic/apyrimidinic endonuclease APE1 in the nucleotide incision repair pathway.Nucleic acids research · 2018Article
- Kinetic Features of 3'-5' Exonuclease Activity of Human AP-Endonuclease APE1.Molecules (Basel, Switzerland) · 2018Article
- Capturing snapshots of APE1 processing DNA damage.Nature structural & molecular biology · 2015Article
- High-resolution crystal structures reveal plasticity in the metal binding site of apurinic/apyrimidinic endonuclease I.Biochemistry · 2014Article
- Cloning and characterization of a wheat homologue of apurinic/apyrimidinic endonuclease Ape1L.PloS one · 2014Article
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- Incorporation of omics analyses into artificial gravity research for space exploration countermeasure development.Metabolomics : Official journal of the Metabolomic SocietyReview
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Apurinic/apyrimidinic endonuclease 1 (APE1) mediates the repair of abasic sites and other DNA lesions and is essential for base-excision repair and strand-break repair pathways. APE1 hydrolyzes the phosphodiester bond at abasic sites, producing 5'-deoxyribose phosphate and the 3'-OH primer needed for repair synthesis. It also has additional repair activities, including the removal of 3'-blocking groups. APE1 is a powerful enzyme that absolutely requires Mg2+, but the stoichiometry and catalytic function of the divalent cation remain unresolved for APE1 and for other enzymes in the DNase I superfamily. Previously reported structures of DNA-free APE1 contained either Sm3+ or Pb2+ in the active site. However, these are poor surrogates for Mg2+ because Sm3+ is not a cofactor and Pb2+ inhibits APE1, and their coordination geometry is expected to differ from that of Mg2+. A crystal structure of human APE1 was solved at 1.92 Å resolution with a single Mg2+ ion in the active site. The structure reveals ideal octahedral coordination of Mg2+ via two carboxylate groups and four water molecules. One residue that coordinates Mg2+ directly and two that bind inner-sphere water molecules are strictly conserved in the DNase I superfamily. This structure, together with a recent structure of the enzyme-product complex, inform on the stoichiometry and the role of Mg2+ in APE1-catalyzed reactions.
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