2B3J

Crystal Structure of Staphylococcus aureus tRNA Adenosine Deaminase, TadA, in Complex with RNA

2B3J の概要

• エントリーDOI: 10.2210/pdb2b3j/pdb
• 分子名称: anticodon stem-loop of t-RNA-Arg2 (nucleotides 27-42), tRNA adenosine deaminase, ZINC ION, ... (5 entities in total)
• 機能のキーワード: mixed alpha-beta, protein-rna complex, rna stem-loop, hydrolase-rna complex, hydrolase/rna
• 由来する生物種: Staphylococcus aureus subsp. aureus Mu50; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 90478.62

構造登録者

Losey, H.C.,Ruthenburg, A.J.,Verdine, G.L. (登録日: 2005-09-20, 公開日: 2006-01-24, 最終更新日: 2024-02-14)

主引用文献

Losey, H.C.,Ruthenburg, A.J.,Verdine, G.L.
Crystal structure of Staphylococcus aureus tRNA adenosine deaminase TadA in complex with RNA.
Nat.Struct.Mol.Biol., 13:153-159, 2006

PubMed Abstract: Bacterial tRNA adenosine deaminases (TadAs) catalyze the hydrolytic deamination of adenosine to inosine at the wobble position of tRNA(Arg2), a process that enables this single tRNA to recognize three different arginine codons in mRNA. In addition, inosine is also introduced at the wobble position of multiple eukaryotic tRNAs. The genes encoding these deaminases are essential in bacteria and yeast, demonstrating the importance of their biological activity. Here we report the crystallization and structure determination to 2.0 A of Staphylococcus aureus TadA bound to the anticodon stem-loop of tRNA(Arg2) bearing nebularine, a non-hydrolyzable adenosine analog, at the wobble position. The cocrystal structure reveals the basis for both sequence and structure specificity in the interactions of TadA with RNA, and it additionally provides insight into the active site architecture that promotes efficient hydrolytic deamination.

PubMed: 16415880
DOI: 10.1038/nsmb1047

実験手法

X-RAY DIFFRACTION (2 Å)