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6KI9

Apo structure of FabMG, novel types of Enoyl-acyl carrier protein reductase

Summary for 6KI9
Entry DOI10.2210/pdb6ki9/pdb
DescriptorFabMG, novel types of Enoyl-acyl carrier protein reductase, 1,2-ETHANEDIOL, TETRAETHYLENE GLYCOL, ... (4 entities in total)
Functional Keywordsenoyl-acyl carrier protein reductase, fabmg, oxidoreductase
Biological sourceuncultured bacterium
Total number of polymer chains3
Total formula weight149775.49
Authors
Kim, S.,Rhee, S. (deposition date: 2019-07-17, release date: 2020-05-20, Last modification date: 2024-03-27)
Primary citationKim, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.64 Å)
Structure validation

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