2ivd

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Image:2ivd.gif

2ivd, resolution 2.30Å

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STRUCTURE OF PROTOPORPHYRINOGEN OXIDASE FROM MYXOCOCCUS XANTHUS WITH ACIFLUORFEN

Overview

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 ... [(full description)]

About this Structure

2IVD is a [Single protein] structure of sequence from [Myxococcus xanthus] with ACJ, FAD, TWN and GOL as [ligands]. Active as [Protoporphyrinogen oxidase], with EC number [1.3.3.4]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Crystal structure of protoporphyrinogen oxidase from Myxococcus xanthus and its complex with the inhibitor acifluorfen., Corradi HR, Corrigall AV, Boix E, Mohan CG, Sturrock ED, Meissner PN, Acharya KR, J Biol Chem. 2006 Dec 15;281(50):38625-33. Epub 2006 Oct 17. PMID:17046834

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