1bk0

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{{STRUCTURE_1bk0| PDB=1bk0 | SCENE= }}
{{STRUCTURE_1bk0| PDB=1bk0 | SCENE= }}
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'''ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (ACV-FE COMPLEX)'''
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===ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (ACV-FE COMPLEX)===
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==Overview==
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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 vacant iron coordination site into which dioxygen can bind. Subsequently, iron-dioxygen and iron-oxo species remove the requisite hydrogens from ACV without the direct assistance of protein residues. The crystal structure of the complex with the dioxygen analogue, NO and ACV bound to the active-site iron supports this hypothesis.
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(as it appears on PubMed at http://www.pubmed.gov), where 9194566 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9194566}}
==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 Fri May 2 11:37:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:17:16 2008''

Revision as of 16:17, 30 June 2008

Image:1bk0.png

Template:STRUCTURE 1bk0

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

Template:ABSTRACT PUBMED 9194566

About this Structure

1BK0 is a Single protein structure of sequence from Emericella nidulans. Full crystallographic information is available from OCA.

Reference

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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