3A4T

Crystal structure of aTrm4 from M.jannaschii with sinefungin

3A4T の概要

• エントリーDOI: 10.2210/pdb3a4t/pdb
• 分子名称: Putative methyltransferase MJ0026, SINEFUNGIN (3 entities in total)
• 機能のキーワード: trna, m5c, rossmann fold, structural genomics, rsgi, riken structural genomics/proteomics initiative, methyltransferase, s-adenosyl-l-methionine, transferase
• 由来する生物種: Methanocaldococcus jannaschii (Methanococcus jannaschii)
• 細胞内の位置: Cytoplasm : Q60343
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 63833.02

構造登録者

Hirano, M.,Kuratani, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2009-07-14, 公開日: 2010-06-30, 最終更新日: 2024-10-23)

主引用文献

Kuratani, M.,Hirano, M.,Goto-Ito, S.,Itoh, Y.,Hikida, Y.,Nishimoto, M.,Sekine, S.,Bessho, Y.,Ito, T.,Grosjean, H.,Yokoyama, S.
Crystal structure of Methanocaldococcus jannaschii Trm4 complexed with sinefungin.
J.Mol.Biol., 401:323-333, 2010

PubMed Abstract: tRNA:m(5)C methyltransferase Trm4 generates the modified nucleotide 5-methylcytidine in archaeal and eukaryotic tRNA molecules, using S-adenosyl-l-methionine (AdoMet) as methyl donor. Most archaea and eukaryotes possess several Trm4 homologs, including those related to diseases, while the archaeon Methanocaldococcus jannaschii has only one gene encoding a Trm4 homolog, MJ0026. The recombinant MJ0026 protein catalyzed AdoMet-dependent methyltransferase activity on tRNA in vitro and was shown to be the M. jannaschii Trm4. We determined the crystal structures of the substrate-free M. jannaschii Trm4 and its complex with sinefungin at 1.27 A and 2.3 A resolutions, respectively. This AdoMet analog is bound in a negatively charged pocket near helix alpha8. This helix can adopt two different conformations, thereby controlling the entry of AdoMet into the active site. Adjacent to the sinefungin-bound pocket, highly conserved residues form a large, positively charged surface, which seems to be suitable for tRNA binding. The structure explains the roles of several conserved residues that were reportedly involved in the enzymatic activity or stability of Trm4p from the yeast Saccharomyces cerevisiae. We also discuss previous genetic and biochemical data on human NSUN2/hTrm4/Misu and archaeal PAB1947 methyltransferase, based on the structure of M. jannaschii Trm4.

PubMed: 20600111
DOI: 10.1016/j.jmb.2010.06.046

実験手法

X-RAY DIFFRACTION (2.3 Å)