7ABB

The truncated structure of the Bottromycin biosynthetic protein SalCYP

7ABB の概要

• エントリーDOI: 10.2210/pdb7abb/pdb
• 分子名称: SalCYP truncation, HEME C (3 entities in total)
• 機能のキーワード: biosynthetic protein, cytochrome, p450, bottromycin
• 由来する生物種: Salinispora tropica
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44399.16

構造登録者

Adam, S.,Koehnke, J. (登録日: 2020-09-07, 公開日: 2020-12-02, 最終更新日: 2024-01-31)

主引用文献

Adam, S.,Franz, L.,Milhim, M.,Bernhardt, R.,Kalinina, O.V.,Koehnke, J.
Characterization of the Stereoselective P450 Enzyme BotCYP Enables the In Vitro Biosynthesis of the Bottromycin Core Scaffold.
J.Am.Chem.Soc., 142:20560-20565, 2020

PubMed Abstract: Bottromycins are ribosomally synthesized and post-translationally modified peptide natural product antibiotics that are effective against high-priority human pathogens such as methicillin-resistant . The total synthesis of bottromycins involves at least 17 steps, with a poor overall yield. Here, we report the characterization of the cytochrome P450 enzyme BotCYP from a bottromycin biosynthetic gene cluster. We determined the structure of a close BotCYP homolog and used our data to conduct the first large-scale survey of P450 enzymes associated with RiPP biosynthetic gene clusters. We demonstrate that BotCYP converts a C-terminal thiazoline to a thiazole via an oxidative decarboxylation reaction and provides stereochemical resolution for the pathway. Our data enable the two-pot production of the bottromycin core scaffold and may allow the rapid generation of bottromycin analogues for compound development.

PubMed: 33249843
DOI: 10.1021/jacs.0c10361

実験手法

X-RAY DIFFRACTION (1.50004339457 Å)