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1YQL

Catalytically inactive hOGG1 crosslinked with 7-deaza-8-azaguanine containing DNA

Summary for 1YQL
Entry DOI10.2210/pdb1yql/pdb
Related1EBM 1KO9 1YQK 1YQM 1YQR
Descriptor5'-D(P*GP*GP*TP*AP*GP*AP*CP*CP*TP*GP*GP*AP*C)-3', 5'-D(P*GP*TP*CP*CP*AP*(PPW)P*GP*TP*CP*TP*AP*C)-3', N-glycosylase/DNA lyase, ... (5 entities in total)
Functional Keywordsdisulfide crosslinking, hydrolase-dna complex, hydrolase/dna
Biological sourceHomo sapiens (human)
Cellular locationNucleus, nucleoplasm. Isoform 1A: Nucleus. Isoform 2A: Mitochondrion: O15527
Total number of polymer chains3
Total formula weight43705.85
Authors
Banerjee, A.,Yang, W.,Karplus, M.,Verdine, G.L. (deposition date: 2005-02-02, release date: 2005-04-05, Last modification date: 2023-11-29)
Primary citationBanerjee, A.,Yang, W.,Karplus, M.,Verdine, G.L.
Structure of a repair enzyme interrogating undamaged DNA elucidates recognition of damaged DNA.
Nature, 434:612-618, 2005
Cited by
PubMed Abstract: How DNA repair proteins distinguish between the rare sites of damage and the vast expanse of normal DNA is poorly understood. Recognizing the mutagenic lesion 8-oxoguanine (oxoG) represents an especially formidable challenge, because this oxidized nucleobase differs by only two atoms from its normal counterpart, guanine (G). Here we report the use of a covalent trapping strategy to capture a human oxoG repair protein, 8-oxoguanine DNA glycosylase I (hOGG1), in the act of interrogating normal DNA. The X-ray structure of the trapped complex features a target G nucleobase extruded from the DNA helix but denied insertion into the lesion recognition pocket of the enzyme. Free energy difference calculations show that both attractive and repulsive interactions have an important role in the preferential binding of oxoG compared with G to the active site. The structure reveals a remarkably effective gate-keeping strategy for lesion discrimination and suggests a mechanism for oxoG insertion into the hOGG1 active site.
PubMed: 15800616
DOI: 10.1038/nature03458
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

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