1OJ4
Ternary complex of 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
Summary for 1OJ4
| Entry DOI | 10.2210/pdb1oj4/pdb |
| Descriptor | 4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE, 4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (5 entities in total) |
| Functional Keywords | transferase, kinase, isoprenoids biosynthesis, ghmp kinase superfamily transferase |
| Biological source | ESCHERICHIA COLI |
| Total number of polymer chains | 2 |
| Total formula weight | 64623.90 |
| Authors | Miallau, L.,Alphey, M.S.,Hunter, W.N. (deposition date: 2003-06-30, release date: 2003-07-31, Last modification date: 2024-10-09) |
| Primary citation | Miallau, L.,Alphey, M.S.,Kemp, L.E.,Leonard, G.A.,Mcsweeney, S.M.,Hecht, S.,Bacher, A.,Eisenreich, W.,Rohdich, F.,Hunter, W.N. Biosynthesis of Isoprenoids: Crystal Structure of 4-Diphosphocytidyl-2C-Methyl-D-Erythritol Kinase Proc.Natl.Acad.Sci.USA, 100:9173-, 2003 Cited by PubMed Abstract: 4-Diphosphocytidyl-2C-methyl-d-erythritol kinase, an essential enzyme in the nonmevalonate pathway of isopentenyl diphosphate and dimethylallyl diphosphate biosynthesis, catalyzes the single ATP-dependent phosphorylation stage affording 4-diphosphocytidyl-2C-methyl-d-erythritol-2-phosphate. The 2-A resolution crystal structure of the Escherichia coli enzyme in a ternary complex with substrate and a nonhydrolyzable ATP analogue reveals the molecular determinants of specificity and catalysis. The enzyme subunit displays the alpha/beta fold characteristic of the galactose kinase/homoserine kinase/mevalonate kinase/phosphomevalonate kinase superfamily, arranged into cofactor and substrate-binding domains with the catalytic center positioned in a deep cleft between domains. Comparisons with related members of this superfamily indicate that the core regions of each domain are conserved, whereas there are significant differences in the substrate-binding pockets. The nonmevalonate pathway is essential in many microbial pathogens and distinct from the mevalonate pathway used by mammals. The high degree of sequence conservation of the enzyme across bacterial species suggests similarities in structure, specificity, and mechanism. Our model therefore provides an accurate template to facilitate the structure-based design of broad-spectrum antimicrobial agents. PubMed: 12878729DOI: 10.1073/PNAS.1533425100 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.01 Å) |
Structure validation
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