5ERG
Crystal structure of the two-subunit tRNA m1A58 methyltransferase TRM6-TRM61 in complex with SAM
5ERG の概要
| エントリーDOI | 10.2210/pdb5erg/pdb |
| 関連するPDBエントリー | 5EQJ |
| 分子名称 | tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6, tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit TRM61, S-ADENOSYLMETHIONINE, ... (4 entities in total) |
| 機能のキーワード | trna, complex, sam, methylation, transferase |
| 由来する生物種 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 詳細 |
| 細胞内の位置 | Nucleus : P41814 P46959 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 100106.61 |
| 構造登録者 | |
| 主引用文献 | Wang, M.,Zhu, Y.,Wang, C.,Fan, X.,Jiang, X.,Ebrahimi, M.,Qiao, Z.,Niu, L.,Teng, M.,Li, X. Crystal structure of the two-subunit tRNA m(1)A58 methyltransferase TRM6-TRM61 from Saccharomyces cerevisiae. Sci Rep, 6:32562-32562, 2016 Cited by PubMed Abstract: The N(1) methylation of adenine at position 58 (m(1)A58) of tRNA is an important post-transcriptional modification, which is vital for maintaining the stability of the initiator methionine tRNAi(Met). In eukaryotes, this modification is performed by the TRM6-TRM61 holoenzyme. To understand the molecular mechanism that underlies the cooperation of TRM6 and TRM61 in the methyl transfer reaction, we determined the crystal structure of TRM6-TRM61 holoenzyme from Saccharomyces cerevisiae in the presence and absence of its methyl donor S-Adenosyl-L-methionine (SAM). In the structures, two TRM6-TRM61 heterodimers assemble as a heterotetramer. Both TRM6 and TRM61 subunits comprise an N-terminal β-barrel domain linked to a C-terminal Rossmann-fold domain. TRM61 functions as the catalytic subunit, containing a methyl donor (SAM) binding pocket. TRM6 diverges from TRM61, lacking the conserved motifs used for binding SAM. However, TRM6 cooperates with TRM61 forming an L-shaped tRNA binding regions. Collectively, our results provide a structural basis for better understanding the m(1)A58 modification of tRNA occurred in Saccharomyces cerevisiae. PubMed: 27582183DOI: 10.1038/srep32562 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.202 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






