6ee1: Difference between revisions

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<StructureSection load='6ee1' size='340' side='right'caption='[[6ee1]], [[Resolution|resolution]] 2.36&Aring;' scene=''>
<StructureSection load='6ee1' size='340' side='right'caption='[[6ee1]], [[Resolution|resolution]] 2.36&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6ee1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycto Mycto]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EE1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EE1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6ee1]] 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=6EE1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EE1 FirstGlance]. <br>
</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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.36&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6edw|6edw]], [[6edz|6edz]]</td></tr>
<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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">icl2, aceA-2, MT1966 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83331 MYCTO])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ee1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ee1 OCA], [https://pdbe.org/6ee1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ee1 RCSB], [https://www.ebi.ac.uk/pdbsum/6ee1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ee1 ProSAT]</span></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=6ee1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ee1 OCA], [http://pdbe.org/6ee1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ee1 RCSB], [http://www.ebi.ac.uk/pdbsum/6ee1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ee1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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> 
[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>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
 
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>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ee1" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Isocitrate lyase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Mycto]]
[[Category: Mycobacterium tuberculosis CDC1551]]
[[Category: Bashiri, G]]
[[Category: Bashiri G]]
[[Category: Bhusal, R]]
[[Category: Bhusal R]]
[[Category: Leung, I]]
[[Category: Leung I]]
[[Category: Lyase]]

Latest revision as of 17:40, 13 March 2024

Crystal structure of Mycobacterium tuberculosis ICL2 in complex with acetyl-CoACrystal structure of Mycobacterium tuberculosis ICL2 in complex with acetyl-CoA

Structural highlights

6ee1 is a 4 chain structure with sequence from Mycobacterium tuberculosis CDC1551. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.36Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2] [3]

References

  1. ↑ Honer Zu Bentrup K, Miczak A, Swenson DL, Russell DG. Characterization of activity and expression of isocitrate lyase in Mycobacterium avium and Mycobacterium tuberculosis. J Bacteriol. 1999 Dec;181(23):7161-7. PMID:10572116
  2. ↑ Munoz-Elias EJ, McKinney JD. Mycobacterium tuberculosis isocitrate lyases 1 and 2 are jointly required for in vivo growth and virulence. Nat Med. 2005 Jun;11(6):638-44. doi: 10.1038/nm1252. Epub 2005 May 15. PMID:15895072 doi:http://dx.doi.org/10.1038/nm1252
  3. ↑ Gould TA, van de Langemheen H, Munoz-Elias EJ, McKinney JD, Sacchettini JC. Dual role of isocitrate lyase 1 in the glyoxylate and methylcitrate cycles in Mycobacterium tuberculosis. Mol Microbiol. 2006 Aug;61(4):940-7. doi: 10.1111/j.1365-2958.2006.05297.x. PMID:16879647 doi:http://dx.doi.org/10.1111/j.1365-2958.2006.05297.x

6ee1, resolution 2.36Å

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