James Davies
@james-s-davies.bsky.social
Researcher interested in how molecules traverse membranes. Structural biology, biochemistry and biophysics.
Pinned
Structural basis of sodium ion-dependent carnitine transport by OCTN2
Nature Communications - Carnitine uptake by OCTN2 supports fatty acid metabolism. Here, authors report cryo-EM structures of human OCTN2, revealing the mechanism of sodium ion-dependent carnitine...
rdcu.be
Our paper on the human carnitine transporter OCTN2 (SLC22A5) is out in @natcomms.nature.com! We solved structures of OCTN2 in multiple states and explored how carnitine transport is Na⁺-dependent, providing a framework for understanding SPCD disease causing variants and drug interactions.
Our paper on the human carnitine transporter OCTN2 (SLC22A5) is out in @natcomms.nature.com! We solved structures of OCTN2 in multiple states and explored how carnitine transport is Na⁺-dependent, providing a framework for understanding SPCD disease causing variants and drug interactions.
Structural basis of sodium ion-dependent carnitine transport by OCTN2
Nature Communications - Carnitine uptake by OCTN2 supports fatty acid metabolism. Here, authors report cryo-EM structures of human OCTN2, revealing the mechanism of sodium ion-dependent carnitine...
rdcu.be
January 8, 2026 at 12:05 AM
Our paper on the human carnitine transporter OCTN2 (SLC22A5) is out in @natcomms.nature.com! We solved structures of OCTN2 in multiple states and explored how carnitine transport is Na⁺-dependent, providing a framework for understanding SPCD disease causing variants and drug interactions.
Reposted by James Davies
🚨My lab is hiring a postdoc!🚨
If you’re interested in working out the mechanism and physiological impact of bacterial lipid transport processes then please apply!
Job advert is here: tinyurl.com/4swddfda
Get in touch by email ([email protected]) for informal enquiries
Please repost!
Thanks!
If you’re interested in working out the mechanism and physiological impact of bacterial lipid transport processes then please apply!
Job advert is here: tinyurl.com/4swddfda
Get in touch by email ([email protected]) for informal enquiries
Please repost!
Thanks!
December 17, 2025 at 2:41 PM
🚨My lab is hiring a postdoc!🚨
If you’re interested in working out the mechanism and physiological impact of bacterial lipid transport processes then please apply!
Job advert is here: tinyurl.com/4swddfda
Get in touch by email ([email protected]) for informal enquiries
Please repost!
Thanks!
If you’re interested in working out the mechanism and physiological impact of bacterial lipid transport processes then please apply!
Job advert is here: tinyurl.com/4swddfda
Get in touch by email ([email protected]) for informal enquiries
Please repost!
Thanks!
Reposted by James Davies
Thrilled to announce a new @natcomms.nature.com paper led by Alastair Stewart and team @victorchang.edu.au with contributions from @mcdevittlab.bsky.social
Using #cryoEM we discovered unique features of the #Pseudomonas aeruginosa ATP synthase including an unexpected role for #zinc in the complex 🦠🔬
Using #cryoEM we discovered unique features of the #Pseudomonas aeruginosa ATP synthase including an unexpected role for #zinc in the complex 🦠🔬
Distinct structural features of Pseudomonas aeruginosa ATP synthase revealed by cryo-electron microscopy - Nature Communications
ATP synthase powers cells by converting proton translocation into energy. Here, authors reveal distinct structural features of the P. aeruginosa ATP synthase that regulate activity and may serve as ta...
doi.org
December 11, 2025 at 1:12 AM
Thrilled to announce a new @natcomms.nature.com paper led by Alastair Stewart and team @victorchang.edu.au with contributions from @mcdevittlab.bsky.social
Using #cryoEM we discovered unique features of the #Pseudomonas aeruginosa ATP synthase including an unexpected role for #zinc in the complex 🦠🔬
Using #cryoEM we discovered unique features of the #Pseudomonas aeruginosa ATP synthase including an unexpected role for #zinc in the complex 🦠🔬
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.
🔗 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...
www.cell.com
November 9, 2025 at 8:45 PM
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.
🔗 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.
Reposted by James Davies
#microsky finally a TRAP transporter that is *not* the Neu5Ac-transporting SiaPQM ;-)
www.cell.com/structure/fu...
www.cell.com/structure/fu...
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...
www.cell.com
November 6, 2025 at 1:29 AM
#microsky finally a TRAP transporter that is *not* the Neu5Ac-transporting SiaPQM ;-)
www.cell.com/structure/fu...
www.cell.com/structure/fu...