1SUS
Crystal structure of alfalfa feruoyl coenzyme A 3-O-methyltransferase
1SUS の概要
| エントリーDOI | 10.2210/pdb1sus/pdb |
| 関連するPDBエントリー | 1sui |
| 分子名称 | Caffeoyl-CoA O-methyltransferase, CALCIUM ION, S-ADENOSYL-L-HOMOCYSTEINE, ... (5 entities in total) |
| 機能のキーワード | rossmann fold, protein-cofactor-substrate complex, o-methyltransferase, transferase |
| 由来する生物種 | Medicago sativa |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 114814.38 |
| 構造登録者 | Ferrer, J.-L.,Zubieta, C.,Dixon, R.A.,Noel, J.P. (登録日: 2004-03-26, 公開日: 2005-03-15, 最終更新日: 2024-02-14) |
| 主引用文献 | Ferrer, J.-L.,Zubieta, C.,Dixon, R.A.,Noel, J.P. Crystal Structures of Alfalfa Caffeoyl Coenzyme A 3-O-Methyltransferase Plant Physiol., 137:1009-1017, 2005 Cited by PubMed Abstract: Caffeoyl coenzyme A 3-O-methyltransferases (CCoAOMTs) are S-adenosyl-l-methionine-dependent O-methyltransferases (OMTs) involved in lignin biosynthesis. Plant CCoAOMTs belong to a distinct family of OMTs, more closely related to the mammalian catechol OMTs than to other plant OMTs. The crystal structure of alfalfa (Medicago sativa) CCoAOMT in complex with the reaction products S-adenosine-l-homocysteine and feruloyl/sinapoyl CoAs presented here belong to a structurally and mechanistically distinct family of plant small molecule OMTs. These structures provide a new understanding of the substrate preferences and the catalytic mechanism accompanying CCoAOMT-mediated O-methylation of CoA-linked phenylpropanoid substrates. PubMed: 15734921DOI: 10.1104/pp.104.048751 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.7 Å) |
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