期刊
SCIENCE
卷 309, 期 5740, 页码 1534-1539出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1113150
关键词
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资金
- NIGMS NIH HHS [GM44073, R01 GM056775, R01 GM044073, GM56775] Funding Source: Medline
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 tRNA(ala) by ADAT1.
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