6KIA

NADH bound structure of FabMG, novel type of Enoyl-acyl carrier protein reductase

6KIA の概要

• エントリーDOI: 10.2210/pdb6kia/pdb
• 分子名称: Enoyl-acyl carrier protein reductase, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: enoyl-acyl carrier protein reductase, fabmg, oxidoreductase
• 由来する生物種: uncultured bacterium
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 150266.14

構造登録者

Kim, S.,Rhee, S. (登録日: 2019-07-17, 公開日: 2020-05-20, 最終更新日: 2024-03-27)

主引用文献

Kim, S.H.,Khan, R.,Choi, K.,Lee, S.W.,Rhee, S.
A triclosan-resistance protein from the soil metagenome is a novel enoyl-acyl carrier protein reductase: Structure-guided functional analysis.
Febs J., 287:4710-4728, 2020

PubMed Abstract: The synthetic biocide triclosan targets enoyl-acyl carrier protein reductase(s) (ENR) in bacterial type II fatty acid biosynthesis. Screening and sequence analyses of the triclosan resistome from the soil metagenome identified a variety of triclosan-resistance ENRs. Interestingly, the mode of triclosan resistance by one hypothetical protein was elusive, mainly due to a lack of sequence similarity with other proteins that mediate triclosan resistance. Here, we carried out a structure-based function prediction of the hypothetical protein, herein referred to as FabMG, and in vivo and in vitro functional analyses. The crystal structure of FabMG showed limited structural homology with FabG and FabI, which are also involved in type II fatty acid synthesis. In vivo complementation and in vitro activity assays indicated that FabMG is functionally a FabI-type ENR that employs NADH as a coenzyme. Variations in the sequence and structure of FabMG are likely responsible for inefficient binding of triclosan, resulting in triclosan resistance. These data unravel a previously uncharacterized FabMG, which is prevalent in various microbes in triclosan-contaminated environments and provide mechanistic insight into triclosan resistance.

PubMed: 32112503
DOI: 10.1111/febs.15267

実験手法

X-RAY DIFFRACTION (1.5979826945 Å)