1IEZ
Solution Structure of 3,4-Dihydroxy-2-Butanone 4-Phosphate Synthase of Riboflavin Biosynthesis
Summary for 1IEZ
| Entry DOI | 10.2210/pdb1iez/pdb |
| Related | 1g57 1g58 |
| Descriptor | 3,4-Dihydroxy-2-Butanone 4-Phosphate Synthase (1 entity in total) |
| Functional Keywords | dihydroxybutanone phosphate synthase, riboflavin biosynthesis, skeletal rearrangement, antimicrobial target, structure based design, isomerase |
| Biological source | Escherichia coli |
| Cellular location | Cell membrane; Peripheral membrane protein (Potential): P0A7J0 |
| Total number of polymer chains | 1 |
| Total formula weight | 23378.46 |
| Authors | Kelly, M.J.S.,Ball, L.J.,Kuhne, R.,Bacher, A.,Oschkinat, H. (deposition date: 2001-04-11, release date: 2001-11-07, Last modification date: 2024-05-01) |
| Primary citation | Kelly, M.J.,Ball, L.J.,Krieger, C.,Yu, Y.,Fischer, M.,Schiffmann, S.,Schmieder, P.,Kuhne, R.,Bermel, W.,Bacher, A.,Richter, G.,Oschkinat, H. The NMR structure of the 47-kDa dimeric enzyme 3,4-dihydroxy-2-butanone-4-phosphate synthase and ligand binding studies reveal the location of the active site. Proc.Natl.Acad.Sci.USA, 98:13025-13030, 2001 Cited by PubMed Abstract: Recent developments in NMR have extended the size range of proteins amenable to structural and functional characterization to include many larger proteins involved in important cellular processes. By applying a combination of residue-specific isotope labeling and protein deuteration strategies tailored to yield specific information, we were able to determine the solution structure and study structure-activity relationships of 3,4-dihydroxy-2-butanone-4-phosphate synthase, a 47-kDa enzyme from the Escherichia coli riboflavin biosynthesis pathway and an attractive target for novel antibiotics. Our investigations of the enzyme's ligand binding by NMR and site-directed mutagenesis yields a conclusive picture of the location and identity of residues directly involved in substrate binding and catalysis. Our studies illustrate the power of state-of-the-art NMR techniques for the structural characterization and investigation of ligand binding in protein complexes approaching the 50-kDa range in solution. PubMed: 11687623DOI: 10.1073/pnas.231323598 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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