2BU9

Isopenicillin N synthase complexed with L-aminoadipoyl-L-cysteinyl-L- hexafluorovaline

Summary for 2BU9

• Entry DOI: 10.2210/pdb2bu9/pdb
• Related: 1BK0 1BLZ 1HB1 1HB2 1HB3 1HB4 1IPS 1OBN 1OC1 1ODM 1ODN 1QIQ 1QJE 1QJF 1UZW 1W03 1W04 1W05 1W06 1W3V 1W3X 2BJS
• Descriptor: ISOPENICILLIN N SYNTHETASE, FE (III) ION, DELTA-(L-ALPHA-AMINOADIPOYL)-L-CYSTEINYL-L-3,3,3,3',3',3'-HEXAFLUOROVALINE, ... (5 entities in total)
• Functional Keywords: b-lactam antibiotic, oxygenase, penicillin biosynthesis, antibiotic biosynthesis, oxidoreductase
• Biological source: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
• Total number of polymer chains: 1
• Total formula weight: 38187.12

Authors

Howard-Jones, A.R.,Rutledge, P.J.,Clifton, I.J.,Adlington, R.M.,Baldwin, J.E. (deposition date: 2005-06-09, release date: 2005-09-15, Last modification date: 2024-05-08)

Primary citation

Howard-Jones, A.R.,Rutledge, P.J.,Clifton, I.J.,Adlington, R.M.,Baldwin, J.E.
Unique Binding of a Non-Natural L,L,L-Substrate by Isopenicillin N Synthase
Biochem.Biophys.Res.Commun., 336:702-, 2005

PubMed Abstract: Isopenicillin N synthase (IPNS) is a non-haem iron oxidase that catalyses the formation of isopenicillin N from the tripeptide delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-valine. In this report, we describe the crystal structure of the enzyme with a non-natural L,L,L-tripeptide substrate, delta-(L-alpha-aminoadipoyl)-L-cysteinyl-L-3,3,3,3',3',3'-hexafluorovaline. This structure reveals a strong binding interaction of the tripeptide within the active site and a unique conformation for the non-natural L,L,L-diastereomer. Taken together, these findings provide a possible rationale for the previously observed inhibitory effects of L,L,L-tripeptide substrates on IPNS activity.

PubMed: 16143309
DOI: 10.1016/J.BBRC.2005.08.155

Experimental method

X-RAY DIFFRACTION (1.3 Å)