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1f8i
From Proteopedia
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CRYSTAL STRUCTURE OF ISOCITRATE LYASE:NITROPROPIONATE:GLYOXYLATE COMPLEX FROM MYCOBACTERIUM TUBERCULOSIS
Overview
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.
About this Structure
1F8I is a Single protein structure of sequence from Mycobacterium tuberculosis with , and as ligands. Active as Isocitrate lyase, with EC number 4.1.3.1 Full crystallographic information is available from OCA.
Reference
Structure of isocitrate lyase, a persistence factor of Mycobacterium tuberculosis., Sharma V, Sharma S, Hoener zu Bentrup K, McKinney JD, Russell DG, Jacobs WR Jr, Sacchettini JC, Nat Struct Biol. 2000 Aug;7(8):663-8. PMID:10932251
Page seeded by OCA on Thu Feb 21 12:35:59 2008
Categories: Isocitrate lyase | Mycobacterium tuberculosis | Single protein | Bentrup, K Hoener zu. | Jr., W R.Jacobs. | McKinney, J D. | Russell, D G. | Sacchettini, J C. | Sharma, S. | Sharma, V. | TBSGC, TB Structural Genomics Consortium. | GLV | MG | SIN | Alpha-beta barrel | Closed conformation | Protein structure initiative | Psi | Structural genomics | Swapped helices | Tb structural genomics consortium | Tbsgc
