한빛사논문
- 조회1,281
Dong Kyu Kim1,†, Hyun Joo Lee1,†, Jiwon Kong2,†, Ha Yeon Cho1, Sunghoon Kim2 and Beom Sik Kang1,*
1School of Life Sciences, BK21 FOUR KNU Creative BioResearch Group, Kyungpook National University, Daegu 41566, Korea and 2Medicinal Bioconvergence Research Center, College of Pharmacy & School of Medicine, Yonsei University, Incheon 21983, Korea
†The authors wish it to be known that, in their opinion, the first three authors should be regarded as Joint First Authors.
*Corresponding author.
Abstract
In mammals, eight aminoacyl-tRNA synthetases (AARSs) and three AARS-interacting multifunctional proteins (AIMPs) form a multi-tRNA synthetase complex (MSC). MSC components possess extension peptides for MSC assembly and specific functions. Human cytosolic methionyl-tRNA synthetase (MRS) has appended peptides at both termini of the catalytic main body. The N-terminal extension includes a glutathione transferase (GST) domain responsible for interacting with AIMP3, and a long linker peptide between the GST and catalytic domains. Herein, we determined crystal structures of the human MRS catalytic main body, and the complex of the GST domain and AIMP3. The structures reveal human-specific structural details of the MRS, and provide a dynamic model for MRS at the level of domain orientation. A movement of zinc knuckles inserted in the catalytic domain is required for MRS catalytic activity. Depending on the position of the GST domain relative to the catalytic main body, MRS can either block or present its tRNA binding site. Since MRS is part of a huge MSC, we propose a dynamic switching between two possible MRS conformations; a closed conformation in which the catalytic domain is compactly attached to the MSC, and an open conformation with a free catalytic domain dissociated from other MSC components.
논문정보
- Research article
- 2021년 06월 (BRIC 등록일 2021-06-15)
- 국내 연구진
- 생명과학 > 구조생물 및 생물물리학
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