1w2a

From Proteopedia

Revision as of 11:29, 30 October 2007

DEACETOXYCEPHALOSPORIN C SYNTHASE (WITH HIS-TAG) COMPLEXED WITH FE(II) AND ETHYLENE GLYCOL

Overview

Deacetoxycephalosporin C synthase (DAOCS) from Streptomyces clavuligerus, catalyses the oxidative ring expansion of the penicillin nucleus into the, nucleus of cephalosporins. The reaction requires dioxygen and, 2-oxoglutarate as co-substrates to create a reactive iron-oxygen, intermediate from a ferrous iron in the active site. The active enzyme is, monomeric in solution. The structure of DAOCS was determined earlier from, merohedrally twinned crystals where the last four C-terminal residues, (308-311) of one molecule penetrate the active site of a neighbouring, molecule, creating a cyclic trimeric structure in the crystal. Shortening, the polypeptide chain from the C terminus by more than four residues, diminishes activity. Here, we describe a new crystal form of DAOCS in, which trimer ... [(full description)]

About this Structure

1W2A is a [Single protein] structure of sequence from [Streptomyces clavuligerus] with FE and EDO 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

Conformational flexibility of the C terminus with implications for substrate binding and catalysis revealed in a new crystal form of deacetoxycephalosporin C synthase., Oster LM, van Scheltinga AC, Valegard K, Hose AM, Dubus A, Hajdu J, Andersson I, J Mol Biol. 2004 Oct 8;343(1):157-71. PMID:15381427

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