James Davies

Congratulations to first author Michael Newton-Vesty and thanks to all of our collaborators across New Zealand, Australia, and Italy who made this possible.

This work extends our understanding of TRAP transporters beyond sialic acid systems, revealing how these sodium-coupled machines recognise and move a different class of substrates.

Functional assays show that the system is Na⁺-driven, and that transport relies on a partner substrate-binding protein (IseP) for delivery and specificity. The membrane transporter alone does not efficiently transport isethionate, so binding is effectively outsourced to its soluble partner.

Structural basis of isethionate transport by a TRAP transporter from a sulfate-reducing bacterium Newton-Vesty et al. used a megabody fiducial to determine the cryo-EM structure of an isethionate TRAP transporter, revealing the substrate and Na+-binding sites. Transport is dependent on Na+ and the...

Check out our new paper:
🔗 www.cell.com/structure/fu...

We explored how sulfate-reducing bacteria import isethionate, a sulfur-containing molecule found in the environment and produced by microbes in the human gut. We captured a structure of the IseQM TRAP transporter in a substrate-bound state.

Structural basis of isethionate transport by a TRAP transporter from a sulfate-reducing bacterium Newton-Vesty et al. used a megabody fiducial to determine the cryo-EM structure of an isethionate TRAP transporter, revealing the substrate and Na+-binding sites. Transport is dependent on Na+ and the...

#microsky finally a TRAP transporter that is *not* the Neu5Ac-transporting SiaPQM ;-)

www.cell.com/structure/fu...