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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Structure of isocitrate lyase, a persistence factor of Mycobacterium tuberculosis.

Isocitrate lyase ( ICL) plays a pivotal role in the persistence of Mycobacterium tuberculosis in mice by sustaining intracellular infection in inflammatory macrophages. The enzyme allows net carbon gain by diverting acetyl-CoA from beta-oxidation of fatty acids into the glyoxylate shunt pathway. Given its potential as a drug target against persistent infections, we solved its structure without ligand and in complex with two inhibitors. Covalent modification of an active site residue, Cys 191, by the inhibitor 3-bromopyruvate traps the enzyme in a catalytic conformation with the active site completely inaccessible to solvent. The structure of a C191S mutant of the enzyme with the inhibitor 3-nitropropionate provides further insight into the reaction mechanism.[1]

References

  1. Structure of isocitrate lyase, a persistence factor of Mycobacterium tuberculosis. Sharma, V., Sharma, S., Hoener zu Bentrup, K., McKinney, J.D., Russell, D.G., Jacobs, W.R., Sacchettini, J.C. Nat. Struct. Biol. (2000) [Pubmed]
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