1ZY7

Crystal structure of the catalytic domain of an adenosine deaminase that acts on RNA (hADAR2) bound to inositol hexakisphosphate (IHP)

1ZY7 の概要

• エントリーDOI: 10.2210/pdb1zy7/pdb
• 分子名称: RNA-specific adenosine deaminase B1, isoform DRADA2a, ZINC ION, INOSITOL HEXAKISPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: alpha/beta deaminase motif, zinc coordination, ionsitol hexakisphosphate, hydrolase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 91557.72

構造登録者

Macbeth, M.R.,Schubert, H.L.,Vandemark, A.P.,Lingam, A.T.,Hill, C.P.,Bass, B.L. (登録日: 2005-06-09, 公開日: 2005-09-13, 最終更新日: 2024-02-14)

主引用文献

Macbeth, M.R.,Schubert, H.L.,Vandemark, A.P.,Lingam, A.T.,Hill, C.P.,Bass, B.L.
Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA editing.
Science, 309:1534-1539, 2005

PubMed Abstract: We report the crystal structure of the catalytic domain of human ADAR2, an RNA editing enzyme, at 1.7 angstrom resolution. The structure reveals a zinc ion in the active site and suggests how the substrate adenosine is recognized. Unexpectedly, inositol hexakisphosphate (IP6) is buried within the enzyme core, contributing to the protein fold. Although there are no reports that adenosine deaminases that act on RNA (ADARs) require a cofactor, we show that IP6 is required for activity. Amino acids that coordinate IP6 in the crystal structure are conserved in some adenosine deaminases that act on transfer RNA (tRNA) (ADATs), related enzymes that edit tRNA. Indeed, IP6 is also essential for in vivo and in vitro deamination of adenosine 37 of tRNAala by ADAT1.

PubMed: 16141067
DOI: 10.1126/science.1113150

実験手法

X-RAY DIFFRACTION (1.7 Å)