1bk0
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ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (ACV-FE COMPLEX)
OverviewOverview
The biosynthesis of penicillin and cephalosporin antibiotics in, microorganisms requires the formation of the bicyclic nucleus of, penicillin. Isopenicillin N synthase (IPNS), a non-haem iron-dependent, oxidase, catalyses the reaction of a tripeptide, delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-valine (ACV), and dioxygen to, form isopenicillin N and two water molecules. Mechanistic studies suggest, the reaction is initiated by ligation of the substrate thiolate to the, iron centre, and proceeds through an enzyme-bound monocyclic intermediate., Here we report the crystal structure of IPNS complexed to ferrous iron and, ACV, determined to 1.3 A resolution. Based on the structure, we propose a, mechanism for penicillin formation that involves ligation of ACV to the, iron centre, creating a ... [(full description)]
About this StructureAbout this Structure
1BK0 is a [Single protein] structure of sequence from [Emericella nidulans] with SO4, FE and ACV as [ligands]. Structure known Active Site: SA. Full crystallographic information is available from [OCA].
ReferenceReference
Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation., Roach PL, Clifton IJ, Hensgens CM, Shibata N, Schofield CJ, Hajdu J, Baldwin JE, Nature. 1997 Jun 19;387(6635):827-30. PMID:9194566
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