1oc1
|
ISOPENICILLIN N SYNTHASE AMINOADIPOYL-CYSTEINYL-AMINOBUTYRATE-FE COMPLEX
OverviewOverview
Isopenicillin N synthase (IPNS) is a non-haem iron(II) oxidase which, catalyses the biosynthesis of isopenicillin N from the tripeptide, delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-valine (ACV). Herein we report, crystallographic studies to investigate the reaction of IPNS with the, truncated substrate analogue, delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-alpha-aminobutyrate (ACAb). It, has been reported previously that this analogue gives rise to three, beta-lactam products when incubated with IPNS: two methyl penams and a, cepham. Crystal structures of the IPNS-Fe(II)-ACAb and IPNS-Fe(II)-ACAb-NO, complexes have now been solved and are reported herein. These structures, and modelling studies based on them shed light on the diminished product, selectivity shown by IPNS in its reaction with ACAb and further, rationalize the presence of certain key residues at the IPNS active site.
About this StructureAbout this Structure
1OC1 is a Single protein structure of sequence from Emericella nidulans with , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Structural studies on the reaction of isopenicillin N synthase with the substrate analogue delta-(l-alpha-aminoadipoyl)-l-cysteinyl-d-alpha-aminobutyrate., Long AJ, Clifton IJ, Roach PL, Baldwin JE, Schofield CJ, Rutledge PJ, Biochem J. 2003 Jun 15;372(Pt 3):687-93. PMID:12622704
Page seeded by OCA on Sun Feb 3 09:55:59 2008