What is it about?
This work provides the first systematic mutational structure-function analysis of a highly conserved amino acid sequence motif of the major facilitator superfamily. We predicted that the alpha-helix formed by the antiporter motif (motif C) is kinked.
Featured Image
Photo by Bill Oxford on Unsplash
Why is it important?
The alpha-helix structure formed by the antiporter motif is widely conserved, from bacteria to humans, and appears to play key functional roles in antimicrobial transporters, including multidrug efflux pumps. The antiporter motif structure may form the basis of novel targets for modulation of multidrug resistance.
Perspectives
Since its publication in 1995, various studies of the antiporter motif have shown that it is a critical element in the antimicrobial transporter cycle, such as serving as a molecular hinge mechanism within multidrug efflux pumps of the major facilitator superfamily. No doubt this work will continue to be of importance in the field of bacterial antimicrobial resistance.
Dr Manuel F Varela
Eastern New Mexico University
Read the Original
This page is a summary of: Mutational analysis and molecular modelling of an amino acid sequence motif conserved in antiporters but not symporters in a transporter superfamily, Molecular Membrane Biology, January 1995, Taylor & Francis,
DOI: 10.3109/09687689509072433.
You can read the full text:
Resources
Contributors
The following have contributed to this page
