5ZW3
Crystal Structure of TrmR from B. subtilis
5ZW3 の概要
| エントリーDOI | 10.2210/pdb5zw3/pdb |
| 分子名称 | Putative O-methyltransferase YrrM, S-ADENOSYL-L-HOMOCYSTEINE, MAGNESIUM ION, ... (4 entities in total) |
| 機能のキーワード | transferase, rna binding protein |
| 由来する生物種 | Bacillus subtilis (strain 168) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 52900.99 |
| 構造登録者 | |
| 主引用文献 | Ryu, H.,Grove, T.L.,Almo, S.C.,Kim, J. Identification of a novel tRNA wobble uridine modifying activity in the biosynthesis of 5-methoxyuridine. Nucleic Acids Res., 46:9160-9169, 2018 Cited by PubMed Abstract: Derivatives of 5-hydroxyuridine (ho5U), such as 5-methoxyuridine (mo5U) and 5-oxyacetyluridine (cmo5U), are ubiquitous modifications of the wobble position of bacterial tRNA that are believed to enhance translational fidelity by the ribosome. In gram-negative bacteria, the last step in the biosynthesis of cmo5U from ho5U involves the unique metabolite carboxy S-adenosylmethionine (Cx-SAM) and the carboxymethyl transferase CmoB. However, the equivalent position in the tRNA of Gram-positive bacteria is instead mo5U, where the methyl group is derived from SAM and installed by an unknown methyltransferase. By utilizing a cmoB-deficient strain of Escherichia coli as a host and assaying for the formation of mo5U in total RNA isolates with methyltransferases of unknown function from Bacillus subtilis, we found that this modification is installed by the enzyme TrmR (formerly known as YrrM). Furthermore, X-ray crystal structures of TrmR with and without the anticodon stemloop of tRNAAla have been determined, which provide insight into both sequence and structure specificity in the interactions of TrmR with tRNA. PubMed: 29982645DOI: 10.1093/nar/gky592 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.27 Å) |
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