Time-resolved cryo-EM reveals conformational trajectory of allosteric activation in isocitrate lyase

Authors

Taka, J., Jung, J., Guo, S., Jiao, W., Kwai, B. X., de Carvalho, L., McNeil, M., Huang, E. Y., Yu, Z., Leung, I. K. H., Bashiri, G.

Abstract

Isocitrate lyase 2 (ICL2) from Mycobacterium tuberculosis undergoes dramatic conformational rearrangements upon binding to the allosteric effector acetyl-CoA. Time resolved cryo EM captured conformational states along the ICL2 activation trajectory, revealing how acetyl CoA binding at the allosteric sites leads to asymmetric, half-of-site activity at the catalytic centres. These findings support a conformational selection model of allostery, whereby acetyl-CoA binding shifts the pre-existing equilibrium towards an active state of the enzyme.

Preprint server: bioRxiv
The authors list and abstract were imported from bioRxiv on 10 Apr 2026.

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