Crystal Structure of tRNA Adenosine Deaminase (TadA) from Aquifex aeolicus
作者： Mitsuo Kuratani , Ryohei Ishii , Yoshitaka Bessho , Ryuya Fukunaga , Toru Sengoku
关键词: Biology 、 Aquifex aeolicus 、 Wobble base pair 、 Cytosine deaminase 、 Stem-loop 、 Adenosine deaminase 、 Cytidine 、 Biochemistry 、 TRNA binding 、 Transfer RNA
摘要: The bacterial tRNA adenosine deaminase (TadA) generates inosine by deaminating the residue at wobble position of tRNAArg-2. This modification is essential for decoding system. In this study, we determined crystal structure Aquifex aeolicus TadA a 1.8-A resolution. first acting on tRNA. A. has an α/β/α three-layered fold and forms homodimer. dimeric completely different from tetrameric yeast CDD1, which deaminates mRNA cytidine, but similar to cytosine deaminase. However, in structure, shapes C-terminal helix regions between β4 β5 strands are quite distinct those large cavity produced. contains many conserved amino acid residues that likely be involved either catalysis or binding. We made docking model with anticodon stem loop.
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