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'''CRYSTAL STRUCTURE OF 3-BROMOPYRUVATE MODIFIED ISOCITRATE LYASE (ICL) FROM MYCOBACTERIUM TUBERCULOSIS''' | '''CRYSTAL STRUCTURE OF 3-BROMOPYRUVATE MODIFIED ISOCITRATE LYASE (ICL) FROM MYCOBACTERIUM TUBERCULOSIS''' | ||
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[[Category: Sharma, V.]] | [[Category: Sharma, V.]] | ||
[[Category: TBSGC, TB Structural Genomics Consortium.]] | [[Category: TBSGC, TB Structural Genomics Consortium.]] | ||
[[Category: | [[Category: Alpha-beta barrel]] | ||
[[Category: | [[Category: Bromopyuvate modification]] | ||
[[Category: | [[Category: Closed conformation]] | ||
[[Category: | [[Category: Helix-swapping]] | ||
[[Category: | [[Category: Protein structure initiative]] | ||
[[Category: | [[Category: Psi]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: | [[Category: Tb structural genomics consortium]] | ||
[[Category: | [[Category: Tbsgc]] | ||
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Revision as of 13:01, 2 May 2008
CRYSTAL STRUCTURE OF 3-BROMOPYRUVATE MODIFIED ISOCITRATE LYASE (ICL) 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
1F8M is a Single protein structure of sequence from Mycobacterium tuberculosis. 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 Fri May 2 16:01:53 2008
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- 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.
- Alpha-beta barrel
- Bromopyuvate modification
- Closed conformation
- Helix-swapping
- Protein structure initiative
- Psi
- Structural genomic
- Tb structural genomics consortium
- Tbsgc
