Structural highlights
Publication Abstract from PubMedIsopenicillin N synthase (IPNS) is a nonheme-Fe(2+)-dependent enzyme that mediates a key step in penicillin biosynthesis. It catalyses the conversion of the tripeptide delta-(l-alpha-aminoadipoyl)-l-cysteine-d-valine (ACV) to isopenicillin N, which is a key precursor to beta-lactam antibiotics. The pa4191 gene in Pseudomonas aeruginosa PAO1 has provisionally been annotated as a member of the IPNS family. In this work, we report the crystal structure of PA4191 from P. aeruginosa (PaIPNS hereafter). The 1.65A resolution PaIPNS structure forms a jelly roll fold and is confirmed to be a member of the IPNS family based on structural homology. A metal centre within the jelly roll consists of the strictly conserved His201, Asp203 and His257 residues. MicroScale Thermophoresis binding analysis confirms that PaIPNS is a metal-binding protein with a strong preference for iron, but that it does not bind the tripeptide ACV. Structural comparison of PaIPNS with a previously reported IPNS-ACV complex structure reveals a restricted binding pocket that is unable to accommodate ACV. Structural characterization of an isopenicillin N synthase family oxygenase from Pseudomonas aeruginosa PAO1.,Zhang H, Che S, Wang R, Liu R, Zhang Q, Bartlam M Biochem Biophys Res Commun. 2019 May 13. pii: S0006-291X(19)30932-5. doi:, 10.1016/j.bbrc.2019.05.062. PMID:31097228[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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