1f61: Difference between revisions
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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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| 1f61, resolution 2.00Å | |||||||||||||
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| Ligands: | MG | ||||||||||||
| 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
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- 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
