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Published online before print July 27, 2007, 10.1110/ps.072972807
Protein Science (2007), 16:2082-2088. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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PROTEIN STRUCTURE REPORT

Biosynthesis of isoprenoids in plants: Structure of the 2C-methyl-D-erithrytol 2,4-cyclodiphosphate synthase from Arabidopsis thaliana. Comparison with the bacterial enzymes

Barbara M. Calisto1, Jordi Perez-Gil2, Maria Bergua2, Jordi Querol-Audi1, Ignacio Fita1, and Santiago Imperial2

1 Institut de Biologia Molecular de Barcelona-CSIC and Institut de Recerca Biomedica, Parc Cientific de Barcelona, 08028 Barcelona, Spain
2 Departament de Bioquimica i Biologia Molecular, Facultat de Biologia, Universitat de Barcelona, 08028 Barcelona, Spain

(RECEIVED May 2, 2007; FINAL REVISION June 6, 2007; ACCEPTED June 6, 2007)

The X-ray crystal structure of the 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (MCS) from Arabidopsis thaliana has been solved at 2.3 Å resolution in complex with a cytidine-5-monophosphate (CMP) molecule. This is the first structure determined of an MCS enzyme from a plant. Major differences between the A. thaliana and bacterial MCS structures are found in the large molecular cavity that forms between subunits and involve residues that are highly conserved among plants. In some bacterial enzymes, the corresponding cavity has been shown to be an isoprenoid diphosphate-like binding pocket, with a proposed feedback-regulatory role. Instead, in the structure from A. thaliana the cavity is unsuited for binding a diphosphate moiety, which suggests a different regulatory mechanism of MCS enzymes between bacteria and plants.

Keywords: plant enzymes; MEP pathway; isoprenoid-binding proteins; cytidine-5-monophosphate; zinc ions


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