6edz

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<StructureSection load='6edz' size='340' side='right'caption='[[6edz]], [[Resolution|resolution]] 2.67&Aring;' scene=''>
<StructureSection load='6edz' size='340' side='right'caption='[[6edz]], [[Resolution|resolution]] 2.67&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6edz]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EDZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EDZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6edz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_CDC1551 Mycobacterium tuberculosis CDC1551]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EDZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EDZ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.67&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6edw|6edw]], [[6ee1|6ee1]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6edz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6edz OCA], [https://pdbe.org/6edz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6edz RCSB], [https://www.ebi.ac.uk/pdbsum/6edz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6edz ProSAT]</span></td></tr>
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<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>
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<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=6edz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6edz OCA], [http://pdbe.org/6edz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6edz RCSB], [http://www.ebi.ac.uk/pdbsum/6edz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6edz ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ACEA2_MYCTO ACEA2_MYCTO]] Involved in the persistence and virulence of M.tuberculosis. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates.<ref>PMID:10572116</ref> <ref>PMID:15895072</ref> <ref>PMID:16879647</ref>
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[https://www.uniprot.org/uniprot/ACEA2_MYCTO ACEA2_MYCTO] Involved in the persistence and virulence of M.tuberculosis. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates.<ref>PMID:10572116</ref> <ref>PMID:15895072</ref> <ref>PMID:16879647</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Isocitrate lyase is important for lipid utilisation by Mycobacterium tuberculosis but its ICL2 isoform is poorly understood. Here we report that binding of the lipid metabolites acetyl-CoA or propionyl-CoA to ICL2 induces a striking structural rearrangement, substantially increasing isocitrate lyase and methylisocitrate lyase activities. Thus, ICL2 plays a pivotal role regulating carbon flux between the tricarboxylic acid (TCA) cycle, glyoxylate shunt and methylcitrate cycle at high lipid concentrations, a mechanism essential for bacterial growth and virulence.
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Acetyl-CoA-mediated activation of Mycobacterium tuberculosis isocitrate lyase 2.,Bhusal RP, Jiao W, Kwai BXC, Reynisson J, Collins AJ, Sperry J, Bashiri G, Leung IKH Nat Commun. 2019 Oct 11;10(1):4639. doi: 10.1038/s41467-019-12614-7. PMID:31604954<ref>PMID:31604954</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6edz" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Isocitrate lyase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bashiri, G]]
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[[Category: Mycobacterium tuberculosis CDC1551]]
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[[Category: Bhusal, R]]
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[[Category: Bashiri G]]
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[[Category: Leung, I]]
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[[Category: Bhusal R]]
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[[Category: Lyase]]
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[[Category: Leung I]]

Current revision

Crystal structure of Mycobacterium tuberculosis ICL2 in complex with acetyl-CoA, form I

PDB ID 6edz

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