Principles of alternating access in multidrug and toxin extrusion (MATE) transporters
By D. P. Claxton, K. Jagessar, Hassane S. Mchaourab. 2021
24 citations recorded by the source corpus.
The multidrug and toxin extrusion (MATE) transporters catalyze active efflux of a broad range of chemically- and structurally-diverse compounds including antimicrobials and chemotherapeutics, thus contributing to multidrug resistance in pathogenic bacteria and cancers. Multiple methodological approaches have been taken to investigate the structural basis of energy transduction and substrate translocation in MATE transporters. Crystal structures representing members from all three MATE subfamilies have been interpreted within the context of an alternating access mechanism that postulates occupation of distinct structural intermediates in a conformational cycle powered by electrochemical ion gradients. Here we review the structural biology of MATE transporters, integrating the crystallographic models with biophysical and computational studies to define the molecular determinants that shape the transport energy landscape. This holistic analysis highlights both shared and disparate structural and functional features within the MATE family, which underpin an emerging theme of mechanistic diversity within the framework of a conserved structural scaffold.
Subfields: Molecular Medicine, Oncology, Pharmacology
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Citations in the corpus
- Sampling alternative conformational states of transporters and receptors with AlphaFold2 (2022, background): “This divergence in performance may stem from the composition of the AF2 training set, which featured the structures of many active GPCRs but no structures, for example, of IF MATEs ( Claxton et al., 2021 ).”