1f61
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1f61.gif|left|200px]] | [[Image:1f61.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1f61", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | | | + | --> |
- | | | + | {{STRUCTURE_1f61| PDB=1f61 | SCENE= }} |
- | + | ||
- | + | ||
- | }} | + | |
'''CRYSTAL STRUCTURE OF ISOCITRATE LYASE FROM MYCOBACTERIUM TUBERCULOSIS''' | '''CRYSTAL STRUCTURE OF ISOCITRATE LYASE FROM MYCOBACTERIUM TUBERCULOSIS''' | ||
Line 34: | Line 31: | ||
[[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: Apo-enzyme]] |
- | [[Category: | + | [[Category: Open conformation]] |
- | [[Category: | + | [[Category: Protein structure initiative]] |
- | [[Category: | + | [[Category: Psi]] |
- | [[Category: | + | [[Category: Structural genomic]] |
- | [[Category: | + | [[Category: Swapped helice]] |
- | [[Category: | + | [[Category: Tb structural genomics consortium]] |
- | [[Category: | + | [[Category: Tbsgc]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:56:50 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 12:56, 2 May 2008
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. 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 15:56:50 2008
Categories: Isocitrate lyase | Mycobacterium tuberculosis | Single protein | Bentrup, K H.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 | Apo-enzyme | Open conformation | Protein structure initiative | Psi | Structural genomic | Swapped helice | Tb structural genomics consortium | Tbsgc