1f8i: Difference between revisions
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|PDB= 1f8i |SIZE=350|CAPTION= <scene name='initialview01'>1f8i</scene>, resolution 2.25Å | |PDB= 1f8i |SIZE=350|CAPTION= <scene name='initialview01'>1f8i</scene>, resolution 2.25Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=GLV:GLYOXYLIC+ACID'>GLV</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG2224 AceA]</span> | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f8i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f8i OCA], [http://www.ebi.ac.uk/pdbsum/1f8i PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1f8i RCSB]</span> | |||
}} | }} | ||
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[[Category: Sharma, V.]] | [[Category: Sharma, V.]] | ||
[[Category: TBSGC, TB Structural Genomics Consortium.]] | [[Category: TBSGC, TB Structural Genomics Consortium.]] | ||
[[Category: alpha-beta barrel]] | [[Category: alpha-beta barrel]] | ||
[[Category: closed conformation]] | [[Category: closed conformation]] | ||
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[[Category: tbsgc]] | [[Category: tbsgc]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 05:52:27 2008'' | ||
Revision as of 03:52, 26 March 2008
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| 1f8i, resolution 2.25Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | GLV, MG, SIN | ||||||||||||
| Activity: | Isocitrate lyase, with EC number 4.1.3.1 | ||||||||||||
| Domains: | AceA | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, JenaLib, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE OF ISOCITRATE LYASE:NITROPROPIONATE:GLYOXYLATE COMPLEX 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
1F8I 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 Wed Mar 26 05:52:27 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
- Closed conformation
- Protein structure initiative
- Psi
- Structural genomic
- Swapped helice
- Tb structural genomics consortium
- Tbsgc
