1oc1: Difference between revisions
No edit summary |
No edit summary |
||
| Line 5: | Line 5: | ||
==Overview== | ==Overview== | ||
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 . | 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 Structure== | ==About this Structure== | ||
1OC1 is a | 1OC1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Emericella_nidulans Emericella nidulans] with FE2, SO4 and ASV as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OC1 OCA]. | ||
==Reference== | ==Reference== | ||
| Line 27: | Line 27: | ||
[[Category: penicillin biosynthesis]] | [[Category: penicillin biosynthesis]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:34:12 2007'' | ||
Revision as of 16:28, 5 November 2007
|
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 FE2, SO4 and ASV as ligands. Structure known Active Site: AC1. 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 Mon Nov 5 15:34:12 2007