🧵Antibiotic resistance is a public health crisis. But viruses called phages have been solving this problem for millennia. New research in @nature.com reveals how 3 different phages attack the same weak spot—a protein called MurJt—potentially leading to a new class of antibiotics.

Structures of bacterial and human phosphoglycosyltransferases bound to a common inhibitor inform selective therapeutics Glycoconjugates facilitate myriad biological processes, including cell–cell recognition and immune response, and they are generated by enzymes that transfer glycans. The orthologs MraY and DPAGT1 are ...

Second, from the Clemons lab at Caltech, we determined high-resolution cryo-EM reconstructions for human and bacterial phosphoglycosyltransferase orthologs with a common inhibitor. www.biorxiv.org/content/10.6...

Nucleotide and metalloid-driven conformational changes in the arsenite efflux ATPase ArsA A common mechanism of arsenic detoxification in bacteria is arsenite (AsIII) efflux facilitated by the ArsAB pump that couples metalloid transport to ATP hydrolysis. The cytoplasmic ATPase component, ...

A new paper from our lab is available at doi.org/10.1101/2025.... The work describes how ArsA, which is involved in arsenic detoxification, utilizes nucleotides to drive dramatic conformational changes—multiple EM structures of a 64kDa protein. Congratulations to Shivansh Mahajan.

It was a pleasure for us. Thanks for making the effort and sharing your exciting work.

That’s a fun crowd.

It was a fun day. Thanks everyone!

A privilege to host Bil Clemons @profbilc.bsky.social at the NIH Intramural Program for the Wednesday Afternoon Lecture Series. A fantastic talk about how phages use proteins to target bacterial cell wall biosynthesis machinery and a truly insightful lesson about inequity in science and society.