1e5i

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(New page: 200px<br /> <applet load="1e5i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e5i, resolution 2.10&Aring;" /> '''DELTA-R306 DEACETOX...)
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Revision as of 14:49, 29 October 2007


1e5i, resolution 2.10Å

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

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

1E5I is a [Single protein] structure of sequence from [Streptomyces clavuligerus] with FE2 and AKG as [ligands]. 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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