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Biosynthesis of isoprenoids in plants: Structure of the 2C‐methyl‐ d ‐erithrytol 2,4‐cyclodiphosphate synthase from Arabidopsis thaliana . Comparison with the bacterial enzymes
Author(s) -
Calisto Barbara M.,
PerezGil Jordi,
Bergua Maria,
QuerolAudi Jordi,
Fita Ignacio,
Imperial Santiago
Publication year - 2007
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.072972807
Subject(s) - arabidopsis thaliana , enzyme , biochemistry , stereochemistry , atp synthase , molecular replacement , chemistry , biosynthesis , biology , gene , mutant
Abstract 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.