2IVE

Structure of protoporphyrinogen oxidase from Myxococcus xanthus

2IVE の概要

• エントリーDOI: 10.2210/pdb2ive/pdb
• 関連するPDBエントリー: 2IVD
• 分子名称: PROTOPORPHYRINOGEN OXIDASE, FLAVIN-ADENINE DINUCLEOTIDE, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: oxidoreductase, protoporphyrinogen oxidase, porphyrin biosynthesis, chlorophyll biosynthesis, fad, porphyria, flavoprotein, heme biosynthesis, haem biosynthesis
• 由来する生物種: MYXOCOCCUS XANTHUS
• 細胞内の位置: Cytoplasm: P56601
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 103980.50

構造登録者

Corradi, H.R.,Corrigall, A.V.,Boix, E.,Mohan, C.G.,Sturrock, E.D.,Meissner, P.N.,Acharya, K.R. (登録日: 2006-06-13, 公開日: 2006-10-17, 最終更新日: 2023-12-13)

主引用文献

Corradi, H.R.,Corrigall, A.V.,Boix, E.,Mohan, C.G.,Sturrock, E.D.,Meissner, P.N.,Acharya, K.R.
Crystal Structure of Protoporphyrinogen Oxidase from Myxococcus Xanthus and its Complex with the Inhibitor Acifluorfen.
J.Biol.Chem., 281:38625-, 2006

PubMed Abstract: Protoporphyrinogen IX oxidase, a monotopic membrane protein, which catalyzes the oxidation of protoporphyrinogen IX to protoporphyrin IX in the heme/chlorophyll biosynthetic pathway, is distributed widely throughout nature. Here we present the structure of protoporphyrinogen IX oxidase from Myxococcus xanthus, an enzyme with similar catalytic properties to human protoporphyrinogen IX oxidase that also binds the common plant herbicide, acifluorfen. In the native structure, the planar porphyrinogen substrate is mimicked by a Tween 20 molecule, tracing three sides of the macrocycle. In contrast, acifluorfen does not mimic the planarity of the substrate but is accommodated by the shape of the binding pocket and held in place by electrostatic and aromatic interactions. A hydrophobic patch surrounded by positively charged residues suggests the position of the membrane anchor, differing from the one proposed for the tobacco mitochondrial protoporphyrinogen oxidase. Interestingly, there is a discrepancy between the dimerization state of the protein in solution and in the crystal. Conserved structural features are discussed in relation to a number of South African variegate porphyria-causing mutations in the human enzyme.

PubMed: 17046834
DOI: 10.1074/JBC.M606640200

実験手法

X-RAY DIFFRACTION (2.7 Å)