@article {70357,
	title = {Time-resolved cryo-EM reveals conformational trajectory of allosteric activation in isocitrate lyase},
	journal = {bioRxiv},
	year = {2026},
	month = {2026 Apr 09},
	abstract = {<p>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.</p>
},
	doi = {10.64898/2026.04.08.716820},
	url = {https://www.biorxiv.org/content/early/2026/04/09/2026.04.08.716820},
	author = {Taka, Jamie and Jung, James and Guo, Shuning and Jiao, Wanting and Kwai, Brooke X. C. and de Carvalho, Luiz Pedro S and McNeil, Matthew and Huang, Evelyn Yu-Wen and Yu, Zhiheng and Leung, Ivanhoe K. H. and Bashiri, Ghader}
}
