1KO9

Native Structure of the Human 8-oxoguanine DNA Glycosylase hOGG1

1KO9 の概要

• エントリーDOI: 10.2210/pdb1ko9/pdb
• 関連するPDBエントリー: 1EBM 1FN7
• 分子名称: 8-oxoguanine DNA glycosylase, SULFATE ION (3 entities in total)
• 機能のキーワード: helix-hairpin-helix dna-glycosylase, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus, nucleoplasm. Isoform 1A: Nucleus. Isoform 2A: Mitochondrion: O15527
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39026.29

構造登録者

Bjoras, M.,Seeberg, E.,Luna, L.,Pearl, L.H.,Barrett, T.E. (登録日: 2001-12-20, 公開日: 2002-01-09, 最終更新日: 2023-08-16)

主引用文献

Bjoras, M.,Seeberg, E.,Luna, L.,Pearl, L.H.,Barrett, T.E.
Reciprocal "flipping" underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase.
J.Mol.Biol., 317:171-177, 2002

PubMed Abstract: Both 8oxo-guanine and formamidopyrimidines are major products of oxidative DNA damage that can result in the fixation of transversion mutations following replication if left unrepaired. These lesions are targeted by the N-DNA glycosylase hOgg1, which catalyses excision of the aberrant base followed by cleavage of the phosphate backbone directly 5' to the resultant abasic site in a context, dependent manner. We present the crystal structure of native hOgg1 refined to 2.15 A resolution that reveals a number of highly significant conformational changes on association with DNA that are clearly required for substrate recognition and specificity. Changes of this magnitude appear to be unique to hOgg1 and have not been observed in any of the DNA-glycosylase structures analysed to date where both native and DNA-bound forms are available. It has been possible to identify a mechanism whereby the catalytic residue Lys 249 is "primed" for nucleophilic attack of the N-glycosidic bond.

PubMed: 11902834
DOI: 10.1006/jmbi.2002.5400

実験手法

X-RAY DIFFRACTION (2.15 Å)