Inositol Hexakisphosphate Is Bound in the ADAR2 Core and Required for RNA Editing
-
- Mark R. Macbeth
- Department of Biochemistry, University of Utah, Salt Lake City, UT 84132, USA.
-
- Heidi L. Schubert
- Department of Biochemistry, University of Utah, Salt Lake City, UT 84132, USA.
-
- Andrew P. VanDemark
- Department of Biochemistry, University of Utah, Salt Lake City, UT 84132, USA.
-
- Arunth T. Lingam
- Department of Biochemistry, University of Utah, Salt Lake City, UT 84132, USA.
-
- Christopher P. Hill
- Department of Biochemistry, University of Utah, Salt Lake City, UT 84132, USA.
-
- Brenda L. Bass
- Department of Biochemistry, University of Utah, Salt Lake City, UT 84132, USA.
書誌事項
- 公開日
- 2005-09-02
- DOI
-
- 10.1126/science.1113150
- 公開者
- American Association for the Advancement of Science (AAAS)
この論文をさがす
説明
<jats:p> 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 (IP <jats:sub>6</jats:sub> ) 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 IP <jats:sub>6</jats:sub> is required for activity. Amino acids that coordinate IP <jats:sub>6</jats:sub> in the crystal structure are conserved in some adenosine deaminases that act on transfer RNA (tRNA) (ADATs), related enzymes that edit tRNA. Indeed, IP <jats:sub>6</jats:sub> is also essential for in vivo and in vitro deamination of adenosine 37 of tRNA <jats:sup>ala</jats:sup> by ADAT1. </jats:p>
収録刊行物
-
- Science
-
Science 309 (5740), 1534-1539, 2005-09-02
American Association for the Advancement of Science (AAAS)