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1qje

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{{STRUCTURE_1qje| PDB=1qje | SCENE= }}
{{STRUCTURE_1qje| PDB=1qje | SCENE= }}
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'''ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (IP1-FE COMPLEX)'''
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===ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (IP1-FE COMPLEX)===
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==Overview==
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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 elucidated by X-ray diffraction. Using the natural substrate ACV, this resulted in the IPNS x Fe2+ x IPN product complex. With the substrate analogue, delta-(L-alpha-aminoadipoyl)-L-cysteinyl-L-S-methylcysteine (ACmC) in the crystal, the reaction cycle was interrupted at the monocyclic stage. These mono- and bicyclic structures support our hypothesis of a two-stage reaction sequence leading to penicillin. Furthermore, the formation of a monocyclic sulphoxide product from ACmC is most simply explained by the interception of a high-valency iron-oxo species.
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(as it appears on PubMed at http://www.pubmed.gov), where 10537113 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10537113}}
==About this Structure==
==About this Structure==
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[[Category: Oxygenase]]
[[Category: Oxygenase]]
[[Category: Penicillin biosynthesis]]
[[Category: Penicillin biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:20:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:46:48 2008''

Revision as of 16:46, 27 July 2008

Image:1qje.png

Template:STRUCTURE 1qje

ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (IP1-FE COMPLEX)

Template:ABSTRACT PUBMED 10537113

About this Structure

1QJE is a Single protein structure of sequence from Emericella nidulans. 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

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