4YYE

Crystal structure of the yeast mitochondrial threonyl-tRNA synthetase (MST1) in complex with the canonical tRNAThr and threonyl sulfamoyl adenylate

4YYE の概要

• エントリーDOI: 10.2210/pdb4yye/pdb
• 関連するPDBエントリー: 3UGQ 3UGT 3UH0 4EO4
• 分子名称: Threonine--tRNA ligase, mitochondrial, tRNA, ZINC ION, ... (6 entities in total)
• 機能のキーワード: aminoacyl-trna synthetase, thrrs, mst1, trna, ribonucleoprotein complex, ligase-rna complex, ligase/rna
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 157014.37

構造登録者

Holman, K.M.,Simonovic, M. (登録日: 2015-03-23, 公開日: 2016-01-06, 最終更新日: 2023-09-27)

主引用文献

Holman, K.M.,Wu, J.,Ling, J.,Simonovic, M.
The crystal structure of yeast mitochondrial ThrRS in complex with the canonical threonine tRNA.
Nucleic Acids Res., 44:1428-1439, 2016

PubMed Abstract: In mitochondria of Saccharomyces cerevisiae, a single aminoacyl-tRNA synthetase (aaRS), MST1, aminoacylates two isoacceptor tRNAs, tRNA1(Thr) and tRNA2(Thr), that harbor anticodon loops of different size and sequence. As a result of this promiscuity, reassignment of the CUN codon box from leucine to threonine is facilitated. However, the mechanism by which a single aaRS binds distinct anticodon loops with high specificity is not well understood. Herein, we present the crystal structure of MST1 in complex with the canonical tRNA2(Thr) and non-hydrolyzable analog of threonyl adenylate. Our structure reveals that the dimeric arrangement of MST1 is essential for binding the 5'-phosphate, the second base pair of the acceptor stem, the first two base pairs of the anticodon stem and the first nucleotide of the variable arm. Further, in contrast to the bacterial ortholog that 'reads' the entire anticodon sequence, MST1 recognizes bases in the second and third position and the nucleotide upstream of the anticodon sequence. We speculate that a flexible loop linking strands β4 and β5 may be allosteric regulator that establishes cross-subunit communication between the aminoacylation and tRNA-binding sites. We also propose that structural features of the anticodon-binding domain in MST1 permit binding of the enlarged anticodon loop of tRNA1(Thr).

PubMed: 26704982
DOI: 10.1093/nar/gkv1501

実験手法

X-RAY DIFFRACTION (2.301 Å)