6JPL

The X-ray structure of yeast tRNA methyltransferase Trm7-Trm734 in complex with S-adenosyl-L-methionine

6JPL の概要

• エントリーDOI: 10.2210/pdb6jpl/pdb
• 分子名称: tRNA (guanosine(34)-2'-O)-methyltransferase non-catalytic subunit TRM734, tRNA (cytidine(34)/guanosine(34)-2'-O)-methyltransferase, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (6 entities in total)
• 機能のキーワード: trna methyltransferase, trna maturation, transferase
• 由来する生物種: Saccharomyces cerevisiae S288c (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 308110.73

構造登録者

Hirata, A.,Okada, K.,Yoshii, K.,Shiraisi, H.,Saijo, S.,Yonezawa, K.,Shimizu, N.,Hori, H. (登録日: 2019-03-27, 公開日: 2019-10-02, 最終更新日: 2024-03-27)

主引用文献

Hirata, A.,Okada, K.,Yoshii, K.,Shiraishi, H.,Saijo, S.,Yonezawa, K.,Shimizu, N.,Hori, H.
Structure of tRNA methyltransferase complex of Trm7 and Trm734 reveals a novel binding interface for tRNA recognition.
Nucleic Acids Res., 47:10942-10955, 2019

PubMed Abstract: The complex between Trm7 and Trm734 (Trm7-Trm734) from Saccharomyces cerevisiae catalyzes 2'-O-methylation at position 34 in tRNA. We report biochemical and structural studies of the Trm7-Trm734 complex. Purified recombinant Trm7-Trm734 preferentially methylates tRNAPhe transcript variants possessing two of three factors (Cm32, m1G37 and pyrimidine34). Therefore, tRNAPhe, tRNATrp and tRNALeu are specifically methylated by Trm7-Trm734. We have solved the crystal structures of the apo and S-adenosyl-L-methionine bound forms of Trm7-Trm734. Small angle X-ray scattering reveals that Trm7-Trm734 exists as a hetero-dimer in solution. Trm7 possesses a Rossmann-fold catalytic domain, while Trm734 consists of three WD40 β-propeller domains (termed BPA, BPB and BPC). BPA and BPC form a unique V-shaped cleft, which docks to Trm7. The C-terminal region of Trm7 is required for binding to Trm734. The D-arm of substrate tRNA is required for methylation by Trm7-Trm734. If the D-arm in tRNAPhe is docked onto the positively charged area of BPB in Trm734, the anticodon-loop is located near the catalytic pocket of Trm7. This model suggests that Trm734 is required for correct positioning of tRNA for methylation. Additionally, a point-mutation in Trm7, which is observed in FTSJ1 (human Trm7 ortholog) of nosyndromic X-linked intellectual disability patients, decreases the methylation activity.

PubMed: 31586407
DOI: 10.1093/nar/gkz856

実験手法

X-RAY DIFFRACTION (2.32 Å)