1oc1: Difference between revisions

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==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 ACAb and further, rationalize the presence of certain key residues at the IPNS active site.
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==
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[[Category: Emericella nidulans]]
[[Category: Emericella nidulans]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Baldwin, J.E.]]
[[Category: Baldwin, J E.]]
[[Category: Clifton, I.J.]]
[[Category: Clifton, I J.]]
[[Category: Long, A.J.]]
[[Category: Long, A J.]]
[[Category: Roach, P.L.]]
[[Category: Roach, P L.]]
[[Category: Rutledge, P.J.]]
[[Category: Rutledge, P J.]]
[[Category: Schofield, C.J.]]
[[Category: Schofield, C J.]]
[[Category: ASV]]
[[Category: ASV]]
[[Category: FE2]]
[[Category: FE2]]
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[[Category: penicillin biosynthesis]]
[[Category: penicillin biosynthesis]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:55:59 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:15:54 2008''

Revision as of 15:15, 21 February 2008

File:1oc1.jpg


1oc1, resolution 2.20Å

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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

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