1ZY7
Crystal structure of the catalytic domain of an adenosine deaminase that acts on RNA (hADAR2) bound to inositol hexakisphosphate (IHP)
Summary for 1ZY7
| Entry DOI | 10.2210/pdb1zy7/pdb |
| Descriptor | RNA-specific adenosine deaminase B1, isoform DRADA2a, ZINC ION, INOSITOL HEXAKISPHOSPHATE, ... (5 entities in total) |
| Functional Keywords | alpha/beta deaminase motif, zinc coordination, ionsitol hexakisphosphate, hydrolase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 91557.72 |
| Authors | Macbeth, M.R.,Schubert, H.L.,Vandemark, A.P.,Lingam, A.T.,Hill, C.P.,Bass, B.L. (deposition date: 2005-06-09, release date: 2005-09-13, Last modification date: 2024-02-14) |
| Primary citation | 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 Cited by 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: 16141067DOI: 10.1126/science.1113150 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
Download full validation report
