7SFP

Crystal structure of OssO, a spirocyclase involved in the biosynthesis of ossamycin

7SFP の概要

• エントリーDOI: 10.2210/pdb7sfp/pdb
• 分子名称: Spirocyclase (2 entities in total)
• 機能のキーワード: cyclase, spyrocyclase, oligomycin, calycin, hydrolase
• 由来する生物種: Streptomyces ossamyceticus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23832.33

構造登録者

Bilyk, O.,Leadlay, P.F.,Dias, M.V.B. (登録日: 2021-10-04, 公開日: 2022-08-17, 最終更新日: 2023-10-18)

主引用文献

Bilyk, O.,Oliveira, G.S.,de Angelo, R.M.,Almeida, M.O.,Honorio, K.M.,Leeper, F.J.,Dias, M.V.B.,Leadlay, P.F.
Enzyme-Catalyzed Spiroacetal Formation in Polyketide Antibiotic Biosynthesis.
J.Am.Chem.Soc., 144:14555-14563, 2022

PubMed Abstract: A key step in the biosynthesis of numerous polyketides is the stereospecific formation of a spiroacetal (spiroketal). We report here that spiroacetal formation in the biosynthesis of the macrocyclic polyketides ossamycin and oligomycin involves catalysis by a novel spiroacetal cyclase. OssO from the ossamycin biosynthetic gene cluster (BGC) is homologous to OlmO, the product of an unannotated gene from the oligomycin BGC. The deletion of abolished oligomycin production and led to the isolation of oligomycin-like metabolites lacking the spiroacetal structure. Purified OlmO catalyzed complete conversion of the major metabolite into oligomycin C. Crystal structures of OssO and OlmO reveal an unusual 10-strand β-barrel. Three conserved polar residues are clustered together in the β-barrel cavity, and site-specific mutation of any of these residues either abolished or substantially diminished OlmO activity, supporting a role for general acid/general base catalysis in spiroacetal formation.

PubMed: 35921248
DOI: 10.1021/jacs.2c03313

実験手法

X-RAY DIFFRACTION (2.2 Å)