1UOF
Deacetoxycephalosporin C synthase complexed with Penicillin G
Summary for 1UOF
| Entry DOI | 10.2210/pdb1uof/pdb |
| Related | 1DCS 1E5H 1E5I 1HJF 1HJG 1RXF 1RXG 1UNB 1UO9 1UOB 1UOG |
| Descriptor | DEACETOXYCEPHALOSPORIN C SYNTHETASE, FE (II) ION, PENICILLIN G, ... (4 entities in total) |
| Functional Keywords | oxidoreductase |
| Biological source | STREPTOMYCES CLAVULIGERUS |
| Total number of polymer chains | 1 |
| Total formula weight | 34981.88 |
| Authors | Valegard, K.,Terwisscha Van scheltinga, A.C.,Dubus, A.,Oster, L.M.,Rhangino, G.,Hajdu, J.,Andersson, I. (deposition date: 2003-09-16, release date: 2004-01-09, Last modification date: 2023-12-13) |
| Primary citation | Valegard, K.,Terwisscha Van Scheltinga, A.C.,Dubus, A.,Ranghino, G.,Oster, L.M.,Hajdu, J.,Andersson, I. The Structural Basis of Cephalosporin Formation in a Mononuclear Ferrous Enzyme Nat.Struct.Mol.Biol., 11:95-, 2004 Cited by PubMed Abstract: Deacetoxycephalosporin-C synthase (DAOCS) is a mononuclear ferrous enzyme that transforms penicillins into cephalosporins by inserting a carbon atom into the penicillin nucleus. In the first half-reaction, dioxygen and 2-oxoglutarate produce a reactive iron-oxygen species, succinate and CO2. The oxidizing iron species subsequently reacts with penicillin to give cephalosporin and water. Here we describe high-resolution structures for ferrous DAOCS in complex with penicillins, the cephalosporin product, the cosubstrate and the coproduct. Steady-state kinetic data, quantum-chemical calculations and the new structures indicate a reaction sequence in which a 'booby-trapped' oxidizing species is formed. This species is stabilized by the negative charge of succinate on the iron. The binding sites of succinate and penicillin overlap, and when penicillin replaces succinate, it removes the stabilizing charge, eliciting oxidative attack on itself. Requisite groups of penicillin are within 1 A of the expected position of a ferryl oxygen in the enzyme-penicillin complex. PubMed: 14718929DOI: 10.1038/NSMB712 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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