Ghader Bashiri

The paper uses time-resolved cryo-EM to show how acetyl-CoA binding induces conformational changes in ICL2, leading to asymmetric catalytic activity.

This paper identifies how acetyl-CoA binding induces allostery in Mycobacterium tuberculosis ICL2, revealing a novel mechanism for enzyme activation and potential therapeutic targets.

The paper identifies a feedback mechanism in Mycobacterium tuberculosis where [2Fe-2S] clusters inhibit sulfide supply by regulating the SufS/SufU complex.

The paper revises the biosynthetic pathway for the cofactor F420 in bacteria by identifying the correct substrate for guanylyltransferases and elucidating the role of the C-terminal domain of FbiB.