AI Article Synopsis
- Isopenicillin N synthase (IPNS) is crucial for penicillin production, converting a specific tripeptide into isopenicillin N, the precursor for β-lactam antibiotics.
- The pa4191 gene in Pseudomonas aeruginosa has been identified as part of the IPNS family, and researchers have determined its crystal structure, revealing a jelly roll fold and confirming its membership in this family.
- The PaIPNS protein binds iron but lacks the capability to bind the tripeptide ACV due to a restricted binding pocket, differentiating it from other known IPNS structures.
Article Abstract
Isopenicillin N synthase (IPNS) is a nonheme-Fe-dependent enzyme that mediates a key step in penicillin biosynthesis. It catalyses the conversion of the tripeptide δ-(l-α-aminoadipoyl)-l-cysteine-d-valine (ACV) to isopenicillin N, which is a key precursor to β-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 1.65 Å 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.
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| http://dx.doi.org/10.1016/j.bbrc.2019.05.062 | DOI Listing |
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