Force-induced unfolding of an antibiotic-bound outer-membrane protein

Albertus Viljoen; Yves F Dufrêne

doi:10.1016/j.str.2022.02.009

Force-induced unfolding of an antibiotic-bound outer-membrane protein

Structure. 2022 Mar 3;30(3):321-323. doi: 10.1016/j.str.2022.02.009.

Authors

Albertus Viljoen¹, Yves F Dufrêne²

Affiliations

¹ Louvain Institute of Biomolecular Science and Technology, Université Catholique de Louvain, Louvain-la-Neuve, Belgium. Electronic address: albertus.viljoen@uclouvain.be.
² Louvain Institute of Biomolecular Science and Technology, Université Catholique de Louvain, Louvain-la-Neuve, Belgium. Electronic address: yves.dufrene@uclouvain.be.

PMID: 35245432
DOI: 10.1016/j.str.2022.02.009

Abstract

In this issue of Structure, Ritzmann et al. characterize the unfolding of the β-barrel assembly machinery component BamA with single-molecule force spectroscopy and reveal how an antibiotic changes BamA's mechanical properties and inhibits its activity. This work helps us understand the effects antibiotics have on Gram-negative outer membrane proteins.

Publication types

Research Support, Non-U.S. Gov't
Comment

MeSH terms

Anti-Bacterial Agents / metabolism
Anti-Bacterial Agents / pharmacology
Bacterial Outer Membrane Proteins / chemistry
Escherichia coli / metabolism
Escherichia coli Proteins* / chemistry
Phenylpropionates

Substances

Anti-Bacterial Agents
Bacterial Outer Membrane Proteins
BamA protein, E coli
Escherichia coli Proteins
Phenylpropionates
darobactin