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1E5I

DELTA-R306 DEACETOXYCEPHALOSPORIN C SYNTHASE COMPLEXED WITH IRON AND 2-OXOGLUTARATE.

Summary for 1E5I
Entry DOI10.2210/pdb1e5i/pdb
Related1DCS 1E5H 1RXF 1RXG
DescriptorDEACETOXYCEPHALOSPORIN C SYNTHASE, FE (II) ION, 2-OXOGLUTARIC ACID, ... (4 entities in total)
Functional Keywordsferrous oxygenase, cephalosporin, 2-oxoglutarate, c-terminus antibiotics, oxidoreductase, oxidative coupling control
Biological sourceSTREPTOMYCES CLAVULIGERUS
Total number of polymer chains1
Total formula weight34247.95
Authors
Lee, H.J.,Lloyd, M.D.,Harlos, K.,Clifton, I.J.,Baldwin, J.E.,Schofield, C.J. (deposition date: 2000-07-26, release date: 2001-07-26, Last modification date: 2023-12-13)
Primary citationLee, H.J.,Lloyd, M.D.,Harlos, K.,Clifton, I.J.,Baldwin, J.E.,Schofield, C.J.
Kinetic and Crystallographic Studies on Deacetoxycephalosporin C Synthase (Daocs)
J.Mol.Biol., 308:937-, 2001
Cited by
PubMed Abstract: Deacetoxycephalosporin C synthase (DAOCS) is an iron(II) and 2-oxoglutarate-dependent oxygenase that catalyzes the conversion of penicillin N to deacetoxycephalosporin C, the committed step in the biosynthesis of cephalosporin antibiotics. The crystal structure of DAOCS revealed that the C terminus of one molecule is inserted into the active site of its neighbor in a cyclical fashion within a trimeric unit. This arrangement has hindered the generation of crystalline enzyme-substrate complexes. Therefore, we constructed a series of DAOCS mutants with modified C termini. Oxidation of 2-oxoglutarate was significantly uncoupled from oxidation of the penicillin substrate in certain truncated mutants. The extent of uncoupling varied with the number of residues deleted and the penicillin substrate used. Crystal structures were determined for the DeltaR306 mutant complexed with iron(II) and 2-oxoglutarate (to 2.10 A) and the DeltaR306A mutant complexed with iron(II), succinate and unhydrated carbon dioxide (to 1.96 A). The latter may mimic a product complex, and supports proposals for a metal-bound CO(2) intermediate during catalysis.
PubMed: 11352583
DOI: 10.1006/JMBI.2001.4649
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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