PDBsum entry 1oc1

Oxidoreductase

PDB id

1oc1

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Contents

			Protein chain

					329 a.a. *

			Ligands

					ASV


					SO4 ×3

			Metals

					FE2

			Waters ×203

* Residue conservation analysis

PDB id:

1oc1

Links

Name:

Oxidoreductase

Title:

Isopenicillin n synthase aminoadipoyl-cysteinyl-aminobutyrate-fe complex

Structure:

Isopenicillin n synthetase. Chain: a. Synonym: isopenicillin n synthase. Engineered: yes

Source:

Emericella nidulans (strain fgsc a4 / atcc 38163 / cbs 112.46 / nrrl 194 / m139). Aspergillus nidulans. Organism_taxid: 227321. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.20Å

R-factor:

0.174

R-free:

0.197

Authors:

A.J.Long,I.J.Clifton,P.L.Roach,J.E.Baldwin,C.J.Schofield,P.J.Rutledge

Key ref:

A.J.Long et al. (2003). Structural studies on the reaction of isopenicillin N synthase with the substrate analogue delta-(l-alpha-aminoadipoyl)-l-cysteinyl-d-alpha-aminobutyrate. Biochem J, 372, 687-693. PubMed id: 12622704

Date:

03-Feb-03

Release date:

02-Feb-04

PROCHECK

	Headers

	References

Protein chain

P05326 (IPNS_EMENI) - Isopenicillin N synthase from Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)

Seq: Struc:					331 a.a. 329 a.a.

Key:

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.1.21.3.1 - isopenicillin-N synthase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Pathway:

Penicillin N and Deacetoxycephalosporin C Biosynthesis

Reaction:

N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 = isopenicillin N + 2 H2O

N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine	+	O2	=	isopenicillin N	+	2 × H2O Bound ligand (Het Group name = ASV) matches with 95.83% similarity

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

	Biochem J 372:687-693 (2003)
PubMed id: 12622704

Structural studies on the reaction of isopenicillin N synthase with the substrate analogue delta-(l-alpha-aminoadipoyl)-l-cysteinyl-d-alpha-aminobutyrate.
A.J.Long, I.J.Clifton, P.L.Roach, J.E.Baldwin, C.J.Schofield, P.J.Rutledge.

ABSTRACT

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.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20078029

C.D.Brown-Marshall, A.R.Diebold, and E.I.Solomon (2010).
Reaction coordinate of isopenicillin N synthase: oxidase versus oxygenase activity.

Biochemistry, 49, 1176-1182.

19598184

W.Ge, I.J.Clifton, A.R.Howard-Jones, J.E.Stok, R.M.Adlington, J.E.Baldwin, and P.J.Rutledge (2009).
Structural studies on the reaction of isopenicillin N synthase with a sterically demanding depsipeptide substrate analogue.

Chembiochem, 10, 2025-2031.

PDB code:

2vcm

17907118

A.C.Stewart, I.J.Clifton, R.M.Adlington, J.E.Baldwin, and P.J.Rutledge (2007).
A cyclobutanone analogue mimics penicillin in binding to isopenicillin N synthase.

Chembiochem, 8, 2003-2007.

PDB code:

2jb4

16444759

A.Daruzzaman, I.J.Clifton, R.M.Adlington, J.E.Baldwin, and P.J.Rutledge (2006).
Unexpected oxidation of a depsipeptide substrate analogue in crystalline isopenicillin N synthase.

Chembiochem, 7, 351-358.

PDB codes:

1w3v 1w3x

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.