1f8i

<table><tr><td colspan='2'>[[1f8i]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F8I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F8I FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLV:GLYOXYLIC+ACID'>GLV</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f8m|1f8m]]</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1f8i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f8i RCSB], [http://www.ebi.ac.uk/pdbsum/1f8i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1f8i ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/ACEA_MYCTU ACEA_MYCTU]] Catalyzes the formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle. May be involved in the assimilation of one-carbon compounds via the isocitrate lyase-positive serine pathway (By similarity).

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:10932251</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1f8i" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Isocitrate lyase]]

[[Category: Myctu]]

[[Category: Bentrup, K Hoener zu]]

[[Category: Jacobs, W R]]

[[Category: McKinney, J D]]

[[Category: Russell, D G]]

[[Category: Sacchettini, J C]]

[[Category: Sharma, S]]

[[Category: Sharma, V]]

[[Category: Tbsgc]]