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Crystal structure of the yeast heterodimeric ADAT2/3 deaminase by Liu, Xiwen; Chen, Ruoyu; Sun, Yujie; Chen, Ran; Zhou, Jie; Tian, Qingnan; Tao, Xuan; Zhang, Zhang; Luo, Guan-zheng; Xie, Wei is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract ## Background The adenosine-to-inosine (A-to-I) editing in anticodons of tRNAs is critical for wobble base-pairing during translation. This modification is produced via deamination on A34 and catalyzed by the adenosine deaminase acting on tRNA (ADAT) enzyme. Eukaryotic ADATs are heterodimers composed of the catalytic subunit ADAT2 and the structural subunit ADAT3, but their molecular assemblies and catalytic mechanisms are largely unclear. ## Results Here, we report a 2.8-Å crystal structure of Saccharomyces cerevisiae ADAT2/3 (ScADAT2/3), revealing its heterodimeric assembly and substrate recognition mechanism. While each subunit clearly contains a domain resembling their prokaryotic homolog TadA, suggesting an evolutionary gene duplication event, they also display accessory domains for additional structural or functional purposes. The N-lobe of ScADAT3 exhibits a positively charged region with a potential role in the recognition and binding of tRNA, supported by our biochemical analysis. Interestingly, ScADAT3 employs its C-terminus to block tRNA’s entry into its pseudo-active site and thus inactivates itself for deamination despite the preservation of a zinc-binding

Who reads Crystal structure of the yeast heterodimeric ADAT2/3 deaminase?

Author

Liu, Xiwen; Chen, Ruoyu; Sun, Yujie; Chen, Ran; Zhou, Jie; Tian, Qingnan; Tao, Xuan; Zhang, Zhang; Luo, Guan-zheng; Xie, Wei

Publisher

BioMed Central; Springer (Biomed Central Ltd.); [London]: BioMed Central, c2003-; Springer Science and Business Media LLC; Society for Mining, Metallurgy and Exploration Inc.; Research Square (ISSN 1741-7007)

Published

2020

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)