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1qiq
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1qiq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qiq, resolution 1.5Å" /> '''ISOPENICILLIN N SYNT...)
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Revision as of 19:24, 29 October 2007
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ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (ACMC FE COMPLEX)
Overview
Isopenicillin N synthase (IPNS), a non-haem iron-dependent oxidase, catalyses the biosynthesis of isopenicillin N (IPN), the precursor of all, penicillins and cephalosporins. The key steps in this reaction are the two, iron-dioxygen-mediated ring closures of the tripeptide, delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-valine (ACV). It has been, proposed that the four-membered beta-lactam ring forms initially, associated with a highly oxidized iron(iv)-oxo (ferryl) moiety, which, subsequently mediates closure of the five-membered thiazolidine ring. Here, we describe observation of the IPNS reaction in crystals by X-ray, crystallography. IPNS Fe2+ substrate crystals were grown anaerobically, exposed to high pressures of oxygen to promote reaction and frozen, and, their structures were ... [(full description)]
About this Structure
1QIQ is a [Single protein] structure of sequence from [Emericella nidulans] with FE, SO4 and ACC as [ligands]. Full crystallographic information is available from [OCA].
Reference
The reaction cycle of isopenicillin N synthase observed by X-ray diffraction., Burzlaff NI, Rutledge PJ, Clifton IJ, Hensgens CM, Pickford M, Adlington RM, Roach PL, Baldwin JE, Nature. 1999 Oct 14;401(6754):721-4. PMID:10537113
Page seeded by OCA on Mon Oct 29 21:29:22 2007
