5dql

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==Crystal Structure of 2-vinyl glyoxylate modified isocitrate lyase from Mycobacterium tuberculosis==
==Crystal Structure of 2-vinyl glyoxylate modified isocitrate lyase from Mycobacterium tuberculosis==
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<StructureSection load='5dql' size='340' side='right' caption='[[5dql]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
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<StructureSection load='5dql' size='340' side='right'caption='[[5dql]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5dql]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DQL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DQL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5dql]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_str._Erdman_=_ATCC_35801 Mycobacterium tuberculosis str. Erdman = ATCC 35801]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DQL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DQL 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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=VGX:4-HYDROXY-2-OXOBUTANOIC+ACID'>VGX</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]] 1.782&#8491;</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=5dql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dql OCA], [http://pdbe.org/5dql PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dql RCSB], [http://www.ebi.ac.uk/pdbsum/5dql PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dql ProSAT]</span></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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=VGX:4-HYDROXY-2-OXOBUTANOIC+ACID'>VGX</scene></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=5dql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dql OCA], [https://pdbe.org/5dql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dql RCSB], [https://www.ebi.ac.uk/pdbsum/5dql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dql ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ACEA1_MYCTE ACEA1_MYCTE]] 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. It also catalyzes the formation of pyruvate and succinate from 2-methylisocitrate, a key step in the methylcitrate cycle (propionate degradation route).<ref>PMID:16689789</ref>
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[https://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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Isocitrate lyase (ICL, types 1 and 2) is the first enzyme of the glyoxylate shunt, an essential pathway for Mycobacterium tuberculosis (Mtb) during the persistent phase of human TB infection. Here, we report 2-vinyl-d-isocitrate (2-VIC) as a mechanism-based inactivator of Mtb ICL1 and ICL2. The enzyme-catalyzed retro-aldol cleavage of 2-VIC unmasks a Michael substrate, 2-vinylglyoxylate, which then forms a slowly reversible, covalent adduct with the thiolate form of active-site Cys191 2-VIC displayed kinetic properties consistent with covalent, mechanism-based inactivation of ICL1 and ICL2 with high efficiency (partition ratio, &lt;1). Analysis of a complex of ICL1:2-VIC by electrospray ionization mass spectrometry and X-ray crystallography confirmed the formation of the predicted covalent S-homopyruvoyl adduct of the active-site Cys191.
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Mechanism-based inactivator of isocitrate lyases 1 and 2 from Mycobacterium tuberculosis.,Pham TV, Murkin AS, Moynihan MM, Harris L, Tyler PC, Shetty N, Sacchettini JC, Huang HL, Meek TD Proc Natl Acad Sci U S A. 2017 Jul 18;114(29):7617-7622. doi:, 10.1073/pnas.1706134114. Epub 2017 Jul 5. PMID:28679637<ref>PMID:28679637</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 5dql" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Huang, H L]]
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[[Category: Large Structures]]
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[[Category: Meek, T D]]
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[[Category: Mycobacterium tuberculosis str. Erdman = ATCC 35801]]
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[[Category: Lyase-lyase inhibitor complex]]
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[[Category: Huang H-L]]
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[[Category: Meek TD]]

Current revision

Crystal Structure of 2-vinyl glyoxylate modified isocitrate lyase from Mycobacterium tuberculosis

PDB ID 5dql

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