1P59

Structure of a non-covalent Endonuclease III-DNA Complex

Summary for 1P59

• Entry DOI: 10.2210/pdb1p59/pdb
• Related: 1ORN 1ORP 2ABK
• Descriptor: 5'-D(*AP*AP*GP*AP*CP*GP*(5IU)P*GP*GP*AP*C)-3', 5'-D(TP*GP*(5IU)P*CP*CP*AP*(3DR)P*GP*(5IU)P*CP*T)-3', Endonuclease III, ... (6 entities in total)
• Functional Keywords: dna repair, dna glycosylase, [4fe-4s] cluster, iron-sulfur cluster, hydrolase-dna complex, hydrolase/dna
• Biological source: Geobacillus stearothermophilus
• Total number of polymer chains: 3
• Total formula weight: 33545.35

Authors

Fromme, J.C.,Verdine, G.L. (deposition date: 2003-04-25, release date: 2003-07-15, Last modification date: 2023-08-16)

Primary citation

Fromme, J.C.,Verdine, G.L.
Structure of a Trapped Endonuclease III-DNA Covalent Intermediate
Embo J., 22:3461-3471, 2003

PubMed Abstract: Nearly all cells express proteins that confer resistance to the mutagenic effects of oxidative DNA damage. The primary defense against the toxicity of oxidative nucleobase lesions in DNA is the base-excision repair (BER) pathway. Endonuclease III (EndoIII) is a [4Fe-4S] cluster-containing DNA glycosylase with repair activity specific for oxidized pyrimidine lesions in duplex DNA. We have determined the crystal structure of a trapped intermediate that represents EndoIII frozen in the act of repairing DNA. The structure of the protein-DNA complex provides insight into the ability of EndoIII to recognize and repair a diverse array of oxidatively damaged bases. This structure also suggests a rationale for the frequent occurrence in certain human cancers of a specific mutation in the related DNA repair protein MYH.

PubMed: 12840008
DOI: 10.1093/emboj/cdg311

Experimental method

X-RAY DIFFRACTION (2.5 Å)