1w77
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The homodimeric 2C-methyl-D-erythritol 4-phosphate cytidylyltransferase | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bacher, A.]] | [[Category: Bacher, A.]] | ||
| - | [[Category: Bond, C | + | [[Category: Bond, C S.]] |
[[Category: Eisenreich, W.]] | [[Category: Eisenreich, W.]] | ||
[[Category: Gabrielsen, M.]] | [[Category: Gabrielsen, M.]] | ||
| - | [[Category: Hunter, W | + | [[Category: Hunter, W N.]] |
[[Category: Kaiser, J.]] | [[Category: Kaiser, J.]] | ||
[[Category: Rohdich, F.]] | [[Category: Rohdich, F.]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:41:10 2008'' |
Revision as of 13:41, 21 February 2008
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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 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.
About this Structure
1W77 is a Single protein structure of sequence from Arabidopsis thaliana with , and as ligands. Active as 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, with EC number 2.7.7.60 Known structural/functional Site: . 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
Page seeded by OCA on Thu Feb 21 15:41:10 2008
Categories: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase | Arabidopsis thaliana | Single protein | Bacher, A. | Bond, C S. | Eisenreich, W. | Gabrielsen, M. | Hunter, W N. | Kaiser, J. | Rohdich, F. | C5P | CD | CU | Cytidylyltransferase | Isoprenoid | Non-mevalonate pathway | Plantherbicide | Transferase
