1WWR
Crystal structure of tRNA adenosine deaminase TadA from Aquifex aeolicus
Summary for 1WWR
| Entry DOI | 10.2210/pdb1wwr/pdb |
| Descriptor | tRNA adenosine deaminase TadA, ZINC ION (3 entities in total) |
| Functional Keywords | homodimer, riken structural genomics/proteomics initiative, rsgi, structural genomics, hydrolase |
| Biological source | Aquifex aeolicus |
| Total number of polymer chains | 4 |
| Total formula weight | 78035.78 |
| Authors | Kuratani, M.,Ishii, R.,Bessho, Y.,Fukunaga, R.,Sengoku, T.,Sekine, S.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2005-01-12, release date: 2005-02-01, Last modification date: 2023-10-25) |
| Primary citation | Kuratani, M.,Ishii, R.,Bessho, Y.,Fukunaga, R.,Sengoku, T.,Shirouzu, M.,Sekine, S.,Yokoyama, S. Crystal Structure of tRNA Adenosine Deaminase (TadA) from Aquifex aeolicus J.Biol.Chem., 280:16002-16008, 2005 Cited by PubMed Abstract: The bacterial tRNA adenosine deaminase (TadA) generates inosine by deaminating the adenosine residue at the wobble position of tRNA(Arg-2). This modification is essential for the decoding system. In this study, we determined the crystal structure of Aquifex aeolicus TadA at a 1.8-A resolution. This is the first structure of a deaminase acting on tRNA. A. aeolicus TadA has an alpha/beta/alpha three-layered fold and forms a homodimer. The A. aeolicus TadA dimeric structure is completely different from the tetrameric structure of yeast CDD1, which deaminates mRNA and cytidine, but is similar to the dimeric structure of yeast cytosine deaminase. However, in the A. aeolicus TadA structure, the shapes of the C-terminal helix and the regions between the beta4 and beta5 strands are quite distinct from those of yeast cytosine deaminase and a large cavity is produced. This cavity contains many conserved amino acid residues that are likely to be involved in either catalysis or tRNA binding. We made a docking model of TadA with the tRNA anticodon stem loop. PubMed: 15677468DOI: 10.1074/jbc.M414541200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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