2B3J

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

Summary for 2B3J

• Entry DOI: 10.2210/pdb2b3j/pdb
• Descriptor: anticodon stem-loop of t-RNA-Arg2 (nucleotides 27-42), tRNA adenosine deaminase, ZINC ION, ... (5 entities in total)
• Functional Keywords: mixed alpha-beta, protein-rna complex, rna stem-loop, hydrolase-rna complex, hydrolase/rna
• Biological source: Staphylococcus aureus subsp. aureus Mu50; More
• Total number of polymer chains: 8
• Total formula weight: 90478.62

Authors

Losey, H.C.,Ruthenburg, A.J.,Verdine, G.L. (deposition date: 2005-09-20, release date: 2006-01-24, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)