1e5h
From Proteopedia
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DELTA-R307A DEACETOXYCEPHALOSPORIN C SYNTHASE COMPLEXED WITH SUCCINATE AND CARBON DIOXIDE
Overview
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.
About this Structure
1E5H is a Single protein structure of sequence from Streptomyces clavuligerus with FE2, SIN and CO2 as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Kinetic and crystallographic studies on deacetoxycephalosporin C synthase (DAOCS)., Lee HJ, Lloyd MD, Harlos K, Clifton IJ, Baldwin JE, Schofield CJ, J Mol Biol. 2001 May 18;308(5):937-48. PMID:11352583
Page seeded by OCA on Tue Dec 18 14:58:05 2007
