1M3H

Crystal Structure of Hogg1 D268E Mutant with Product Oligonucleotide

1M3H の概要

• エントリーDOI: 10.2210/pdb1m3h/pdb
• 関連するPDBエントリー: 1EBM 1M3Q
• 分子名称: 5'-D(P*GP*GP*TP*AP*GP*AP*CP*CP*TP*GP*GP*AP*CP*GP*C)-3', 5'-D(P*GP*CP*GP*TP*CP*CP*AP*(DDX))-3', 5'-D(P*GP*TP*CP*TP*AP*CP*C)-3', ... (6 entities in total)
• 機能のキーワード: protein-dna complex, end product, dna repair, dna glycosylase, mutant, enzyme, hydrolase-dna complex, hydrolase/dna
• 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: 4
• 化学式量合計: 44687.29

構造登録者

Chung, S.J.,Verdine, G.L. (登録日: 2002-06-27, 公開日: 2004-04-20, 最終更新日: 2024-02-14)

主引用文献

Chung, S.J.,Verdine, G.L.
Structures of End Products Resulting from Lesion Processing by a DNA Glycosylase/Lyase
Chem.Biol., 11:1643-1649, 2004

PubMed Abstract: DNA glycosylase/lyases initiate the repair of damaged nucleobases in the genome by catalyzing excision of aberrant nucleobases and nicking of the lesion-containing DNA strand. Nearly all of these proteins have the unusual property of remaining tightly bound in vitro to the end products of the reaction cascade. We have taken advantage of this property to crystallize and structurally characterize the end product resulting from complete DNA processing by a catalytically active mutant form of human 8-oxoguanine DNA glycosylase (D268E hOgg1). The resulting structure is consistent with the currently accepted catalytic mechanism for the protein. Unexpectedly, however, soaking of a nucleobase analog into the crystals results in religation of the DNA backbone in situ.

PubMed: 15610848
DOI: 10.1016/j.chembiol.2004.09.014

実験手法

X-RAY DIFFRACTION (2.05 Å)