1odn
From Proteopedia
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ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (OXYGEN-EXPOSED PRODUCT FROM ANAEROBIC AC-VINYLGLYCINE FE COMPLEX)
Overview
Isopenicillin N synthase (IPNS) catalyses conversion of the linear, tripeptide delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-valine (ACV) to, isopenicillin N (IPN), the central step in biosynthesis of the beta-lactam, antibiotics. The unsaturated substrate analogue, delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-vinylglycine (ACvG) has, previously been incubated with IPNS and single product was isolated, a, 2-alpha-hydroxymethyl isopenicillin N (HMPen), formed via a monooxygenase, mode of reactivity. ACvG has now been crystallised with IPNS and the, structure of the anaerobic IPNS:Fe(II):ACvG complex determined to 1.15 A, resolution. Furthermore, by exposing the anaerobically grown crystals to, high-pressure oxygen gas, a structure corresponding to the bicyclic, product HMPen has been obtained ... [(full description)]
About this Structure
1ODN is a [Single protein] structure of sequence from [Emericella nidulans] with SO4, FE2 and APV as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Crystallographic studies on the reaction of isopenicillin N synthase with an unsaturated substrate analogue., Elkins JM, Rutledge PJ, Burzlaff NI, Clifton IJ, Adlington RM, Roach PL, Baldwin JE, Org Biomol Chem. 2003 May 7;1(9):1455-60. PMID:12926272
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