5LOG
Crystal Structure of SafC from Myxococcus xanthus bound to SAM
5LOG の概要
| エントリーDOI | 10.2210/pdb5log/pdb |
| 分子名称 | Putative O-methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE, MAGNESIUM ION, ... (6 entities in total) |
| 機能のキーワード | o-methyl transferase, sam, transferase |
| 由来する生物種 | Myxococcus xanthus |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 53147.58 |
| 構造登録者 | |
| 主引用文献 | Siegrist, J.,Netzer, J.,Mordhorst, S.,Karst, L.,Gerhardt, S.,Einsle, O.,Richter, M.,Andexer, J.N. Functional and structural characterisation of a bacterial O-methyltransferase and factors determining regioselectivity. FEBS Lett., 591:312-321, 2017 Cited by PubMed Abstract: Mg -dependent catechol-O-methyltransferases occur in animals as well as in bacteria, fungi and plants, often with a pronounced selectivity towards one of the substrate's hydroxyl groups. Here, we show that the bacterial MxSafC exhibits excellent regioselectivity for para as well as for meta methylation, depending on the substrate's characteristics. The crystal structure of MxSafC was solved in apo and in holo form. The structure complexed with a full set of substrates clearly illustrates the plasticity of the active site region. The awareness that a wide range of factors influences the regioselectivity will aid the further development of catechol-O-methyltransferases as well as other methyltransferases as selective and efficient biocatalysts for chemical synthesis. PubMed: 27990630DOI: 10.1002/1873-3468.12530 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.01 Å) |
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