1QBJ

CRYSTAL STRUCTURE OF THE ZALPHA Z-DNA COMPLEX

1QBJ の概要

• エントリーDOI: 10.2210/pdb1qbj/pdb
• 分子名称: DNA (5'-D(*TP*CP*GP*CP*GP*CP*G)-3'), PROTEIN (DOUBLE-STRANDED RNA SPECIFIC ADENOSINE DEAMINASE (ADAR1)) (3 entities in total)
• 機能のキーワード: protein-z-dna complex, hydrolase-dna complex, hydrolase/dna
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: P55265
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 33350.07

構造登録者

Schwartz, T.,Rould, M.A.,Rich, A. (登録日: 1999-04-22, 公開日: 1999-07-02, 最終更新日: 2024-02-14)

主引用文献

Schwartz, T.,Rould, M.A.,Lowenhaupt, K.,Herbert, A.,Rich, A.
Crystal structure of the Zalpha domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA.
Science, 284:1841-1845, 1999

PubMed Abstract: The editing enzyme double-stranded RNA adenosine deaminase includes a DNA binding domain, Zalpha, which is specific for left-handed Z-DNA. The 2.1 angstrom crystal structure of Zalpha complexed to DNA reveals that the substrate is in the left-handed Z conformation. The contacts between Zalpha and Z-DNA are made primarily with the "zigzag" sugar-phosphate backbone, which provides a basis for the specificity for the Z conformation. A single base contact is observed to guanine in the syn conformation, characteristic of Z-DNA. Intriguingly, the helix-turn-helix motif, frequently used to recognize B-DNA, is used by Zalpha to contact Z-DNA.

PubMed: 10364558
DOI: 10.1126/science.284.5421.1841

実験手法

X-RAY DIFFRACTION (2.1 Å)