Titratable residues that drive RND efflux: Insights from molecular simulations
Year: 2024
Type: review
Abstract: The resistance-nodulation-division efflux machinery confers antimicrobial resistance to Gram-negative bacteria by actively pumping antibiotics out of the cell. The protein complex is powered by proton motive force; however, the proton transfer mechanism itself and indeed even its stoichiometry is still unclear. Here we review computational studies from the last decade that focus on elucidating the number of protons transferred per conformational cycle of the pump. Given the difficulties in studying proton movement using even state-of-the-art structural biology methods, the contributions from computational studies have been invaluable from a mechanistic perspective.
Source: QRB Discovery
DOI: 10.1017/qrd.2024.6
Authors: Robert Clark, Kahlan E. Newman, Syma Khalid
Institutions: University of Oxford, University of Southampton
Language: English
Subfield: Microbiology (medical)
Field: Medicine
Domain: Health Sciences
Open Access status: gold
Estimated APC paid: $3,450
Awards: G1091649970, DTP Bid Led by University of Oxford, The UK High-End Computing Consortium for Biomolecular Simulation, Identifying the Molecular Determinants of Ferredoxin Transport into the Periplasm of Pectobacterium spp., G2620866968, The UK High-End Computing Consortium for Biomolecular Simulation, G5267706263, DTP Bid Led by University of Oxford, G693515516, MOLSImage: Combining Simulations and Imaging to Deliver Next Generation Tools for Studying Bacterial Cell Envelopes., G8969537021, HECBioSim: The UK High End Computing Consortium for Biomolecular Simulation.
OpenAlex ID: W4393388126