1NKU

NMR Solution Structure of Zinc-binding protein 3-methyladenine DNA glycosylase I (TAG)

1NKU の概要

• エントリーDOI: 10.2210/pdb1nku/pdb
• 関連するPDBエントリー: 1LMZ
• NMR情報: BMRB: 5668
• 分子名称: 3-Methyladenine Dna Glycosylase I (TAG), ZINC ION (2 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21203.54

構造登録者

Kwon, K.,Cao, C.,Stivers, J.T. (登録日: 2003-01-03, 公開日: 2003-06-03, 最終更新日: 2024-05-22)

主引用文献

Kwon, K.,Cao, C.,Stivers, J.T.
A Novel Zinc Snap Motif Conveys Structural Stability to 3-Methyladenine DNA Glycosylase I
J.Biol.Chem., 278:19442-19446, 2003

PubMed Abstract: The Escherichia coli 3-methyladenine DNA glycosylase I (TAG) is a DNA repair enzyme that excises 3-methyladenine in DNA and is the smallest member of the helix-hairpin-helix (HhH) superfamily of DNA glycosylases. Despite many studies over the last 25 years, there has been no suggestion that TAG was a metalloprotein. However, here we establish by heteronuclear NMR and other spectroscopic methods that TAG binds 1 eq of Zn2+ extremely tightly. A family of refined NMR structures shows that 4 conserved residues contributed from the amino- and carboxyl-terminal regions of TAG (Cys4, His17, His175, and Cys179) form a Zn2+ binding site. The Zn2+ ion serves to tether the otherwise unstructured amino- and carboxyl-terminal regions of TAG. We propose that this unexpected "zinc snap" motif in the TAG family (CX(12-17)HX(approximately 150)HX(3)C) serves to stabilize the HhH domain thereby mimicking the functional role of protein-protein interactions in larger HhH superfamily members.

PubMed: 12654914
DOI: 10.1074/jbc.M300934200

実験手法

SOLUTION NMR