1w77

From Proteopedia

2C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE (ISPD) FROM ARABIDOPSIS THALIANA

Overview

The homodimeric 2C-methyl-D-erythritol 4-phosphate cytidylyltransferase, contributes to the nonmevalonate pathway of isoprenoid biosynthesis. The, crystal structure of the catalytic domain of the recombinant enzyme, derived from the plant Arabidopsis thaliana has been solved by molecular, replacement and refined to 2.0 A resolution. The structure contains, cytidine monophosphate bound in the active site, a ligand that has been, acquired from the bacterial expression system, and this observation, suggests a mechanism for feedback regulation of enzyme activity., Comparisons with bacterial enzyme structures, in particular the enzyme, from Escherichia coli, indicate that whilst individual subunits overlay, well, the arrangement of subunits in each functional dimer is different., That distinct ... [(full description)]

About this Structure

1W77 is a [Single protein] structure of sequence from [Arabidopsis thaliana] with CD, CU and C5P as [ligands]. Active as [[1]], with EC number [2.7.7.60]. Full crystallographic information is available from [OCA].

Reference

The crystal structure of a plant 2C-methyl-D-erythritol 4-phosphate cytidylyltransferase exhibits a distinct quaternary structure compared to bacterial homologues and a possible role in feedback regulation for cytidine monophosphate., Gabrielsen M, Kaiser J, Rohdich F, Eisenreich W, Laupitz R, Bacher A, Bond CS, Hunter WN, FEBS J. 2006 Mar;273(5):1065-73. PMID:16478479

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