1f61
From Proteopedia
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- | [[Image:1f61.gif|left|200px]] | + | [[Image:1f61.gif|left|200px]] |
- | + | ||
- | '''CRYSTAL STRUCTURE OF ISOCITRATE LYASE FROM MYCOBACTERIUM TUBERCULOSIS''' | + | {{Structure |
+ | |PDB= 1f61 |SIZE=350|CAPTION= <scene name='initialview01'>1f61</scene>, resolution 2.00Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/Isocitrate_lyase Isocitrate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.1 4.1.3.1] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''CRYSTAL STRUCTURE OF ISOCITRATE LYASE FROM MYCOBACTERIUM TUBERCULOSIS''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1F61 is a [ | + | 1F61 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F61 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10932251 10932251] |
[[Category: Isocitrate lyase]] | [[Category: Isocitrate lyase]] | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
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[[Category: protein structure initiative]] | [[Category: protein structure initiative]] | ||
[[Category: psi]] | [[Category: psi]] | ||
- | [[Category: structural | + | [[Category: structural genomic]] |
- | [[Category: swapped | + | [[Category: swapped helice]] |
[[Category: tb structural genomics consortium]] | [[Category: tb structural genomics consortium]] | ||
[[Category: tbsgc]] | [[Category: tbsgc]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:04:54 2008'' |
Revision as of 09:05, 20 March 2008
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, resolution 2.00Å | |||||||
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Ligands: | |||||||
Activity: | Isocitrate lyase, with EC number 4.1.3.1 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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 Thu Mar 20 11:04:54 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. | MG | Alpha-beta barrel | Apo-enzyme | Open conformation | Protein structure initiative | Psi | Structural genomic | Swapped helice | Tb structural genomics consortium | Tbsgc