6EE1

Crystal structure of Mycobacterium tuberculosis ICL2 in complex with acetyl-CoA

Summary for 6EE1

Entry DOI	10.2210/pdb6ee1/pdb
Related	6EDW 6EDZ
Descriptor	Isocitrate lyase 2, ACETYL COENZYME *A, MAGNESIUM ION, ... (4 entities in total)
Functional Keywords	lyase
Biological source	Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Total number of polymer chains	4
Total formula weight	353735.41
Authors	Bashiri, G.,Bhusal, R.,Leung, I. (deposition date: 2018-08-12, release date: 2019-08-14, Last modification date: 2024-03-13)
Primary citation	Bhusal, R.P.,Jiao, W.,Kwai, B.X.C.,Reynisson, J.,Collins, A.J.,Sperry, J.,Bashiri, G.,Leung, I.K.H. Acetyl-CoA-mediated activation of Mycobacterium tuberculosis isocitrate lyase 2. Nat Commun, 10:4639-4639, 2019 Cited by PubMed Abstract: Isocitrate lyase is important for lipid utilisation by Mycobacterium tuberculosis but its ICL2 isoform is poorly understood. Here we report that binding of the lipid metabolites acetyl-CoA or propionyl-CoA to ICL2 induces a striking structural rearrangement, substantially increasing isocitrate lyase and methylisocitrate lyase activities. Thus, ICL2 plays a pivotal role regulating carbon flux between the tricarboxylic acid (TCA) cycle, glyoxylate shunt and methylcitrate cycle at high lipid concentrations, a mechanism essential for bacterial growth and virulence. PubMed: 31604954 DOI: 10.1038/s41467-019-12614-7 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.36 Å)

Structure validation