6xpp: Difference between revisions
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==Crystal structure of itaconate modified Mycobaterium tuberculosis isocitrate lyase== | |||
<StructureSection load='6xpp' size='340' side='right'caption='[[6xpp]], [[Resolution|resolution]] 1.55Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6xpp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XPP FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ITN:2-METHYLIDENEBUTANEDIOIC+ACID'>ITN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=6xpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xpp OCA], [https://pdbe.org/6xpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xpp RCSB], [https://www.ebi.ac.uk/pdbsum/6xpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xpp ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Itaconate is a mammalian antimicrobial metabolite that inhibits the isocitrate lyases (ICLs) of Mycobacterium tuberculosis. Herein, we report that ICLs form a covalent adduct with itaconate through their catalytic cysteine residue. These results reveal atomic details of itaconate inhibition and provide insights into the catalytic mechanism of ICLs. | |||
Itaconate is a covalent inhibitor of the Mycobacterium tuberculosis isocitrate lyase.,Kwai BXC, Collins AJ, Middleditch MJ, Sperry J, Bashiri G, Leung IKH RSC Med Chem. 2020 Oct 19;12(1):57-61. doi: 10.1039/d0md00301h. eCollection 2021 , Jan 1. PMID:34046597<ref>PMID:34046597</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6xpp" style="background-color:#fffaf0;"></div> | ||
[[Category: Bashiri | == References == | ||
[[Category: Leung | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mycobacterium tuberculosis H37Rv]] | |||
[[Category: Bashiri G]] | |||
[[Category: Kwai BXC]] | |||
[[Category: Leung IKH]] | |||
Latest revision as of 14:58, 18 October 2023
Crystal structure of itaconate modified Mycobaterium tuberculosis isocitrate lyase
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