Tyrosine-targeted covalent inhibition of a tRNA synthetase aided by zinc ion

Hang Qiao; Mingyu Xia; Yiyuan Cheng; Jintong Zhou; Li Zheng; Wei Li; Jing Wang; Pengfei Fang

doi:10.1038/s42003-023-04517-7

Communications Biology (Jan 2023)

Tyrosine-targeted covalent inhibition of a tRNA synthetase aided by zinc ion

Hang Qiao,
Mingyu Xia,
Yiyuan Cheng,
Jintong Zhou,
Li Zheng,
Wei Li,
Jing Wang,
Pengfei Fang

Affiliations

Hang Qiao: State Key Laboratory of Bioorganic and Natural Products Chemistry, Center for Excellence in Molecular Synthesis, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences, Chinese Academy of Sciences
Mingyu Xia: State Key Laboratory of Bioorganic and Natural Products Chemistry, Center for Excellence in Molecular Synthesis, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences, Chinese Academy of Sciences
Yiyuan Cheng: State Key Laboratory of Bioorganic and Natural Products Chemistry, Center for Excellence in Molecular Synthesis, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences, Chinese Academy of Sciences
Jintong Zhou: State Key Laboratory of Bioorganic and Natural Products Chemistry, Center for Excellence in Molecular Synthesis, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences, Chinese Academy of Sciences
Li Zheng: State Key Laboratory of Bioorganic and Natural Products Chemistry, Center for Excellence in Molecular Synthesis, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences, Chinese Academy of Sciences
Wei Li: Department of Medicinal Chemistry, School of Pharmacy, China Pharmaceutical University
Jing Wang: State Key Laboratory of Bioorganic and Natural Products Chemistry, Center for Excellence in Molecular Synthesis, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences, Chinese Academy of Sciences
Pengfei Fang: State Key Laboratory of Bioorganic and Natural Products Chemistry, Center for Excellence in Molecular Synthesis, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences, Chinese Academy of Sciences

DOI: https://doi.org/10.1038/s42003-023-04517-7
Journal volume & issue: Vol. 6, no. 1
pp. 1 – 8

Abstract

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Structures of E. coli threonyl-tRNA synthetase in complex with natural product obafluorin (OB) reveal that OB is a unique covalent inhibitor.

Published in Communications Biology

ISSN: 2399-3642 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science: Biology (General)
Website: https://www.nature.com/commsbio/

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