1orp
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(New page: 200px<br /><applet load="1orp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1orp, resolution 2.20Å" /> '''Structure of a Trapp...)
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Revision as of 23:12, 24 November 2007
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Structure of a Trapped Endonuclease III-DNA Covalent Intermediate: Estranged-Adenine Complex
Overview
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.
About this Structure
1ORP is a Protein complex structure of sequences from Geobacillus stearothermophilus with NA and SF4 as ligands. Full crystallographic information is available from OCA.
Reference
Structure of a trapped endonuclease III-DNA covalent intermediate., Fromme JC, Verdine GL, EMBO J. 2003 Jul 1;22(13):3461-71. PMID:12840008[[Category: [4fe-4s] cluster]]
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