6JYV

Structure of an isopenicillin N synthase from Pseudomonas aeruginosa PAO1

6JYV の概要

• エントリーDOI: 10.2210/pdb6jyv/pdb
• 分子名称: Probable iron/ascorbate oxidoreductase, SODIUM ION (3 entities in total)
• 機能のキーワード: iron binding; isopenicillin n synthase; beta-lactam antibiotic synthesis, metal binding protein
• 由来する生物種: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 75841.58

構造登録者

Hao, Z.,Che, S.,Wang, R.,Liu, R.,Zhang, Q.,Bartlam, M. (登録日: 2019-04-28, 公開日: 2019-05-22, 最終更新日: 2023-11-22)

主引用文献

Zhang, H.,Che, S.,Wang, R.,Liu, R.,Zhang, Q.,Bartlam, M.
Structural characterization of an isopenicillin N synthase family oxygenase from Pseudomonas aeruginosa PAO1.
Biochem.Biophys.Res.Commun., 514:1031-1036, 2019

PubMed 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.

PubMed: 31097228
DOI: 10.1016/j.bbrc.2019.05.062

実験手法

X-RAY DIFFRACTION (1.651 Å)