Justin Di Trani
banner
justinditrani.bsky.social
Justin Di Trani
@justinditrani.bsky.social
Assistant Professor at University of Alberta. Interests in cryoEM, enzymology, and electron transport chain proteins. he/him.
https://sites.google.com/ualberta.ca/theditranigroup/home
https://scholar.google.ca/citations?user=LeG-9koAAAAJ&hl=en
Reposted by Justin Di Trani
Thrilled to announce my first PhD publication in Nature Comms! We determined structures of the Tad pilus ATPase CpaF from Caulobacter. We use these structures to propose how CpaF employs a rotary mechanism of catalysis to drive Tad pilus assembly.
www.nature.com/articles/s41...
Conformational changes in the motor ATPase CpaF facilitate a rotary mechanism of Tad pilus assembly - Nature Communications
The bacterial Tad pilus extends and retracts using a single bifunctional ATPase CpaF. Here, the authors employ cryo-EM, fluorescent microscopy, and AlphaFold modelling to propose how a rotary mechanis...
www.nature.com
April 24, 2025 at 3:29 AM
Reposted by Justin Di Trani
Now published J. Med. Chem! @zestytoast.bsky.social's structure of type II NADH dehydrogenase from mycobacteria. A promising drug target for TB & other mycobacterial infections, Yingke demonstrates how an inhibitor can block transfer of electrons from NADH to the ETC.
pubs.acs.org/doi/full/10....
Structure of Mycobacterial NDH-2 Bound to a 2-Mercapto-Quinazolinone Inhibitor
Mycobacterial type II NADH dehydrogenase (NDH-2) is a promising drug target because of its central role in energy metabolism in Mycobacterium tuberculosis and other pathogens, and because it lacks a k...
pubs.acs.org
March 21, 2025 at 4:55 PM
Reposted by Justin Di Trani
🚨 Amazing Opportunity 🚨
U Alberta is looking for a director for their new #cryoEM facility
Support excellent researchers (who are really nice people) using state-of-the-art infrastructure.
+ reasonable cost of living
+ near some of most beautiful places in world
+ 🇨🇦
apps.ualberta.ca/careers/post...
February 22, 2025 at 2:47 AM
Reposted by Justin Di Trani
Most protein complexes are born only once. V-ATPase assembles over and over as part of its regulatory mechanism, enabled by RAVE (regulator of ATPase of vacuoles and endosomes)
@hanlinw222.bsky.social's 1st struct of RAVE bound to a partial V1 complex now out in PNAS.
www.pnas.org/doi/10.1073/...
December 3, 2024 at 7:34 PM