2PMP
Structure of 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase from the isoprenoid biosynthetic pathway of Arabidopsis thaliana
Summary for 2PMP
| Entry DOI | 10.2210/pdb2pmp/pdb |
| Related | 1GX1 1IV1 1JN1 |
| Descriptor | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, ZINC ION, PHOSPHATE ION, ... (6 entities in total) |
| Functional Keywords | plant enzymes, arabidopsis thaliana, mep pathway, isoprenoid-binding proteins, cmp, zinc ions, lyase |
| Biological source | Arabidopsis thaliana (thale cress) |
| Cellular location | Plastid, chloroplast stroma : Q9CAK8 |
| Total number of polymer chains | 1 |
| Total formula weight | 17868.11 |
| Authors | Calisto, B.M.,Perez-Gil, J.,Querol-Audi, J.,Fita, I.,Imperial, S. (deposition date: 2007-04-23, release date: 2007-09-18, Last modification date: 2023-08-30) |
| Primary citation | Calisto, B.M.,Perez-Gil, J.,Bergua, M.,Querol-Audi, J.,Fita, I.,Imperial, S. Biosynthesis of isoprenoids in plants: Structure of the 2C-methyl-D-erithrytol 2,4-cyclodiphosphate synthase from Arabidopsis thaliana. Comparison with the bacterial enzymes. Protein Sci., 16:2082-2088, 2007 Cited by PubMed 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 A 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. PubMed: 17660251DOI: 10.1110/ps.072972807 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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