1w06
From Proteopedia
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[[Category: penicillin biosynthesis]] | [[Category: penicillin biosynthesis]] | ||
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Revision as of 14:15, 30 October 2007
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ISOPENICILLIN N SYNTHASE AMINOADIPOYL-CYSTEINYL-ALANINE-FE NO COMPLEX
Overview
Isopenicillin N synthase (IPNS), a non-heme iron(II)-dependent oxidase, catalyzes conversion of the tripeptide, delta-(l-alpha-aminoadipoyl)-l-cysteinyl-d-valine (ACV) to bicyclic, isopenicillin N (IPN), concomitant with the reduction of dioxygen to two, molecules of water. Incubation of the "truncated"substrate analogues, delta-(l-alpha-aminoadipoyl)-l-cysteinyl-glycine (ACG) and, delta-(l-alpha-aminoadipoyl)-l-cysteinyl-d-alanine (ACA) with IPNS has, previously been shown to afford acyclic products, in which the substrate, cysteinyl residue has undergone a two-electron oxidation. We report X-ray, crystal structures for the anaerobic IPNS/Fe(II)/ACG and IPNS/Fe(II)/ACA, complexes, both in the absence and presence of the dioxygen analogue, nitric oxide. The overall protein structures are ... [(full description)]
About this Structure
1W06 is a [Single protein] structure of sequence from [Emericella nidulans] with FE2, SO4, W05 and NO as [ligands]. Active as [Isopenicillin-N synthase], with EC number [1.21.3.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Structural studies on the reaction of isopenicillin N synthase with the truncated substrate analogues delta-(L-alpha-aminoadipoyl)-L-cysteinyl-glycine and delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-alanine., Long AJ, Clifton IJ, Roach PL, Baldwin JE, Rutledge PJ, Schofield CJ, Biochemistry. 2005 May 3;44(17):6619-28. PMID:15850395
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