1uo9
From Proteopedia
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DEACETOXYCEPHALOSPORIN C SYNTHASE COMPLEXED WITH SUCCINATE
Overview
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 ... [(full description)]
About this Structure
1UO9 is a [Single protein] structure of sequence from [Streptomyces clavuligerus] with FE2 and SIN as [ligands]. Active as [Deacetoxycephalosporin-C synthase], with EC number [1.14.20.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
The structural basis of cephalosporin formation in a mononuclear ferrous enzyme., Valegard K, Terwisscha van Scheltinga AC, Dubus A, Ranghino G, Oster LM, Hajdu J, Andersson I, Nat Struct Mol Biol. 2004 Jan;11(1):95-101. Epub 2003 Dec 29. PMID:14718929
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