1bk0
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1bk0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bk0, resolution 1.3Å" /> '''ISOPENICILLIN N SYNT...)
Next diff →
Revision as of 19:30, 29 October 2007
|
ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (ACV-FE COMPLEX)
Overview
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 Structure
1BK0 is a [Single protein] structure of sequence from [Emericella nidulans] with SO4, FE and ACV as [ligands]. 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
Page seeded by OCA on Mon Oct 29 21:34:48 2007
