1zy7
From Proteopedia
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'''Crystal structure of the catalytic domain of an adenosine deaminase that acts on RNA (hADAR2) bound to inositol hexakisphosphate (IHP)''' | '''Crystal structure of the catalytic domain of an adenosine deaminase that acts on RNA (hADAR2) bound to inositol hexakisphosphate (IHP)''' | ||
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[[Category: Schubert, H L.]] | [[Category: Schubert, H L.]] | ||
[[Category: Vandemark, A P.]] | [[Category: Vandemark, A P.]] | ||
| - | [[Category: | + | [[Category: Alpha/beta deaminase motif]] |
| - | [[Category: | + | [[Category: Ionsitol hexakisphosphate]] |
| - | [[Category: | + | [[Category: Zinc coordination]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:13:35 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 15:13, 3 May 2008
Crystal structure of the catalytic domain of an adenosine deaminase that acts on RNA (hADAR2) bound to inositol hexakisphosphate (IHP)
Overview
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.
About this Structure
1ZY7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA editing., Macbeth MR, Schubert HL, Vandemark AP, Lingam AT, Hill CP, Bass BL, Science. 2005 Sep 2;309(5740):1534-9. PMID:16141067 Page seeded by OCA on Sat May 3 18:13:35 2008
