Finally, we propose a catalytic scheme that employs two separate coordination positions for the acceptor phosphate within the catalytic domain, and a reaction mechanism that likely operates in all similar enzymes of the polyprenyl phosphate glycosyltransferase family. 8/n

And, with the help of Mariana Bunoro-Batista and @pstansfeld.bsky.social we perform detailed atomistic simulations with both donor and acceptor substrates to fully describe substrate binding and identify catalytic residues in this enzyme. 7/n

With the help of Bertie Ansell and @pstansfeld.bsky.social, we perform coarse-grained simulations to show that the acceptor lipid UndP threads between the juxtamembrane helices of an ArnC protomer to reach the catalytic GT-A domain. 6/n

WIth the help of Jason Kaelber, we perform a comparison of the two apo ArnC datasets collected on a 200kV Talos Arctica and a 300kV Titan Krios microscope using duplicate grids, to examine whether a higher quality microscope/detector can meaningfully improve the reconstruction for this sample. 5/n

We describe a conformational transition that occurs upon binding of the partial substrate UDP, moving the catalytic GT-A domain closer to the membrane. 4/n

For the UDP-bound state, we observed clear non-protein density within the binding cavity of the catalytic GT-A domain, which we modeled as UDP coordinated by a Mn2+ metal ion. 3/n

We determine the #cryoEM structures of ArnC in lipid nanodiscs: an apo conformation at 2.74Å (Krios dataset) and 2.79Å (Arctica dataset), and a UDP-bound conformation at 2.96Å (Arctica dataset). 2/n

Hello everyone! I joined Bluesky some months back but I finally decided to become more active here. I am a structural biologist studying membrane enzymes and ion channels. I am a newish PI, having started my lab in 2019. In Newark we operate a Tundra cryo-TEM. Here is a recent picture of our team: