PDBsum entry 2jb4

Oxidoreductase

PDB id

2jb4

Loading ...

Contents

			Protein chain

					329 a.a. *

			Ligands

					A14


					SO4 ×2


					GOL

			Metals

					_FE

			Waters ×403

* Residue conservation analysis

PDB id:

2jb4

Links

Name:

Oxidoreductase

Title:

Isopenicillin n synthase with a 2-thiabicycloheptan-6-one product analogue

Structure:

Isopenicillin n synthase. Chain: a. Synonym: ipns. Engineered: yes

Source:

Emericella nidulans (strain fgsc a4 / atcc 38163 / cbs 112.46 / nrrl 194 / m139). Aspergillus nidulans. Organism_taxid: 227321. Gene: ipna, ips, an2622. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.30Å

R-factor:

0.154

R-free:

0.176

Authors:

A.C.Stewart,I.J.Clifton,R.M.Adlington,J.E.Baldwin,P.J.Rutledge

Key ref:

A.C.Stewart et al. (2007). A cyclobutanone analogue mimics penicillin in binding to isopenicillin N synthase. Chembiochem, 8, 2003-2007. PubMed id: 17907118 DOI: 10.1002/cbic.200700176

Date:

01-Dec-06

Release date:

16-Oct-07

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:

PfamA domain

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 = A14) matches with 92.00% similarity

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

Added reference

DOI no: 10.1002/cbic.200700176	Chembiochem 8:2003-2007 (2007)
PubMed id: 17907118

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

ABSTRACT

A carbocyclic analogue of the beta-lactam antibiotic isopenicillin N (IPN) has been synthesised and cocrystallised with isopenicillin N synthase (IPNS), the central enzyme in the biosynthesis of penicillin antibiotics. The crystal structure of the IPNS-cyclobutanone complex reveals an active site environment similar to that seen in the enzyme-product complex generated by turnover of the natural substrate within the crystalline protein. The IPNS-cyclobutanone structure demonstrates that the product analogue is tethered to the protein by hydrogen bonding and salt bridge interactions with its carboxylate groups, as seen previously for the natural substrate and product. Furthermore, the successful cocrystallisation of this analogue with IPNS provides firm structural evidence for the utility of such cyclobutanone derivatives as hydrolytically stable analogues of bicyclic beta-lactams.

Literature references that cite this PDB file's key reference

PubMed id

Reference

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

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.