1QYC

Crystal structures of pinoresinol-lariciresinol and phenylcoumaran benzylic ether reductases, and their relationship to isoflavone reductases

1QYC の概要

• エントリーDOI: 10.2210/pdb1qyc/pdb
• 関連するPDBエントリー: 1qyd
• 分子名称: phenylcoumaran benzylic ether reductase PT1 (2 entities in total)
• 機能のキーワード: nadph-dependent aromatic alcohol reductases, pcber, plr, ifr, lignans, isoflavonoids, plant protein
• 由来する生物種: Pinus taeda (loblolly pine)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67126.34

構造登録者

Min, T.,Kasahara, H.,Bedgar, D.L.,Youn, B.,Lawrence, P.K.,Gang, D.R.,Halls, S.C.,Park, H.,Hilsenbeck, J.L.,Davin, L.B.,Kang, C. (登録日: 2003-09-10, 公開日: 2003-11-04, 最終更新日: 2024-02-14)

主引用文献

Min, T.,Kasahara, H.,Bedgar, D.L.,Youn, B.,Lawrence, P.K.,Gang, D.R.,Halls, S.C.,Park, H.,Hilsenbeck, J.L.,Davin, L.B.,Lewis, N.G.,Kang, C.
Crystal structures of pinoresinol-lariciresinol and phenylcoumaran benzylic ether reductases and their relationship to isoflavone reductases.
J.Biol.Chem., 278:50714-50723, 2003

PubMed Abstract: Despite the importance of plant lignans and isoflavonoids in human health protection (e.g. for both treatment and prevention of onset of various cancers) as well as in plant biology (e.g. in defense functions and in heartwood development), systematic studies on the enzymes involved in their biosynthesis have only recently begun. In this investigation, three NADPH-dependent aromatic alcohol reductases were comprehensively studied, namely pinoresinol-lariciresinol reductase (PLR), phenylcoumaran benzylic ether reductase (PCBER), and isoflavone reductase (IFR), which are involved in central steps to the various important bioactive lignans and isoflavonoids. Of particular interest was in determining how differing regio- and enantiospecificities are achieved with the different enzymes, despite each apparently going through similar enone intermediates. Initially, the three-dimensional x-ray crystal structures of both PLR_Tp1 and PCBER_Pt1 were solved and refined to 2.5 and 2.2 A resolutions, respectively. Not only do they share high gene sequence similarity, but their structures are similar, having a continuous alpha/beta NADPH-binding domain and a smaller substrate-binding domain. IFR (whose crystal structure is not yet obtained) was also compared (modeled) with PLR and PCBER and was deduced to have the same overall basic structure. The basis for the distinct enantio-specific and regio-specific reactions of PCBER, PLR, and IFR, as well as the reaction mechanism and participating residues involved (as identified by site-directed mutagenesis), are discussed.

PubMed: 13129921
DOI: 10.1074/jbc.M308493200

実験手法

X-RAY DIFFRACTION (2.2 Å)