8BIJ
O-Methyltransferase Plu4894 (mutant I88M, W91L, C97Y, S142L, G146V, Y258M, L270F, S309Y) in complex with SAH
8BIJ の概要
| エントリーDOI | 10.2210/pdb8bij/pdb |
| 関連するPDBエントリー | 8BIE |
| 分子名称 | Methyltransferase Plu4894 mutant I88M, W91L, C97Y, S142L, G146V, Y258M, L270F, S309Y, S-ADENOSYL-L-HOMOCYSTEINE, 1,2-ETHANEDIOL, ... (6 entities in total) |
| 機能のキーワード | methyltransferase, polyketide, anthraquinone, transferase |
| 由来する生物種 | Photorhabdus laumondii subsp. laumondii TTO1 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 73442.95 |
| 構造登録者 | |
| 主引用文献 | Huber, E.M.,Kreling, L.,Heinrich, A.K.,Dunnebacke, M.,Pothig, A.,Bode, H.B.,Groll, M. A set of closely related methyltransferases for site-specific tailoring of anthraquinone pigments. Structure, 31:573-, 2023 Cited by PubMed Abstract: Modification of the polyketide anthraquinone AQ-256 in the entomopathogenic Photorhabdus luminescens involves several O-methylations, but the biosynthetic gene cluster antA-I lacks corresponding tailoring enzymes. We here describe the identification of five putative, highly homologous O-methyltransferases encoded in the genome of P. luminescens. Activity assays in vitro and deletion experiments in vivo revealed that three of them account for anthraquinone tailoring by producing three monomethylated and two dimethylated species of AQ-256. X-ray structures of all five enzymes indicate high structural and mechanistic similarity. As confirmed by structure-based mutagenesis, a conserved histidine at the active site likely functions as a general base for substrate deprotonation and subsequent methyl transfer in all enzymes. Eight complex structures with AQ-256 as well as mono- and dimethylated derivatives confirm the substrate specificity patterns found in vitro and visualize how single amino acid differences in the active-site pockets impact substrate orientation and govern site-specific methylation. PubMed: 36963398DOI: 10.1016/j.str.2023.03.001 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.55 Å) |
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