TAILIEUCHUNG - Báo cáo khoa học: 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

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 thalianahas been solved by molecular replace-ment and refined to A˚ resolution. | ềFEBS Journal 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 Mads Gabrielsen1 Johannes Kaiser2 Felix Rohdich2 Wolfgang Eisenreich2 Ralf Laupitz2 Adelbert Bacher2 Charles S. Bond1 and William N. Hunter1 1 Division of BiologicalChemistry and Molecular Microbiology Schoolof Life Sciences University of Dundee UK 2 Institut fur Organische Chemie und Biochemie Technische Universitat Munchen Garching Germany Keywords Arabidopsis thaliana cytidylyltransferase herbicide nonmevalonate pathway Correspondence W. N. Hunter Division of Biological Chemistry and Molecular Microbiology Schoolof Life Sciences University of Dundee Dundee DD1 5EH UK Fax 44 1382 345764 Tel 44 1382 345745 E-mail Received 2 August 2005 revised 31 December 2005 accepted 9 January 2006 doi 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 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 .

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