1f61

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Revision as of 12:31, 20 November 2007

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spinqualitylabelsall models 1f61, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF ISOCITRATE LYASE 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

1F61 is a Single protein structure of sequence from Mycobacterium tuberculosis with MG as ligand. 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

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