1YQL
Catalytically inactive hOGG1 crosslinked with 7-deaza-8-azaguanine containing DNA
Summary for 1YQL
Entry DOI | 10.2210/pdb1yql/pdb |
Related | 1EBM 1KO9 1YQK 1YQM 1YQR |
Descriptor | 5'-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 Keywords | disulfide crosslinking, hydrolase-dna complex, hydrolase/dna |
Biological source | Homo sapiens (human) |
Cellular location | Nucleus, nucleoplasm. Isoform 1A: Nucleus. Isoform 2A: Mitochondrion: O15527 |
Total number of polymer chains | 3 |
Total formula weight | 43705.85 |
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 citation | Banerjee, 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: 15800616DOI: 10.1038/nature03458 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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