1W77

2C-methyl-D-erythritol 4-phosphate cytidylyltransferase (IspD) from Arabidopsis thaliana

Summary for 1W77

• Entry DOI: 10.2210/pdb1w77/pdb
• Descriptor: 2C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE, CADMIUM ION, COPPER (II) ION, ... (5 entities in total)
• Functional Keywords: plantherbicide, cytidylyltransferase, arabidopsis thaliana, non-mevalonate pathway, isoprenoid, transferase
• Biological source: ARABIDOPSIS THALIANA (MOUSE-EAR CRESS)
• Total number of polymer chains: 1
• Total formula weight: 26190.10

Authors

Gabrielsen, M.,Kaiser, J.,Rohdich, F.,Eisenreich, W.,Bacher, A.,Bond, C.S.,Hunter, W.N. (deposition date: 2004-08-30, release date: 2006-02-21, Last modification date: 2023-12-13)

Primary citation

Gabrielsen, M.,Kaiser, J.,Rohdich, F.,Eisenreich, W.,Laupitz, R.,Bacher, A.,Bond, C.S.,Hunter, W.N.
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.
FEBS J., 273:1065-, 2006

PubMed Abstract: 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 quaternary structures are available, in conjunction with the observation that the protein structure contains localized areas of disorder, suggests that conformational flexibility may contribute to the function of this enzyme.

PubMed: 16478479
DOI: 10.1111/J.1742-4658.2006.05133.X

Experimental method

X-RAY DIFFRACTION (2 Å)