1e5h

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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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Revision as of 13:01, 30 October 2007


1e5h, resolution 1.96Å

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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 ... [(full description)]

About this Structure

1E5H is a [Single protein] structure of sequence from [Streptomyces clavuligerus] with FE2, SIN and CO2 as [ligands]. Structure known Active Site: FE. 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

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