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==human glyoxalase I (with C-ter His tag) in complex with TLSC702== | ==human glyoxalase I (with C-ter His tag) in complex with TLSC702== | ||
<StructureSection load='7wt0' size='340' side='right'caption='[[7wt0]]' scene=''> | <StructureSection load='7wt0' size='340' side='right'caption='[[7wt0]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WT0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WT0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7wt0]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WT0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WT0 FirstGlance]. <br> | ||
</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=7wt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wt0 OCA], [https://pdbe.org/7wt0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wt0 RCSB], [https://www.ebi.ac.uk/pdbsum/7wt0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wt0 ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5ZO:(~{E})-3-(1,3-benzothiazol-2-yl)-4-(4-methoxyphenyl)but-3-enoic+acid'>5ZO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lactoylglutathione_lyase Lactoylglutathione lyase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.5 4.4.1.5] </span></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=7wt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wt0 OCA], [https://pdbe.org/7wt0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wt0 RCSB], [https://www.ebi.ac.uk/pdbsum/7wt0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wt0 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/LGUL_HUMAN LGUL_HUMAN]] Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B.<ref>PMID:19199007</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Human glyoxalase I (hGLO I) is an enzyme for detoxification of methylglyoxal (MG) and has been considered an attractive target for the development of new anticancer drugs. In our previous report, the GLO I inhibitor TLSC702 induced apoptosis in tumor cells. Here, we determined the crystal structures of hGLO I and its complex with TLSC702. In the complex, the carboxyl O atom of TLSC702 is coordinated to Zn(2+) , and TLSC702 mainly shows van der Waals interaction with hydrophobic residues. In the inhibitor-unbound structure, glycerol, which has similar functional groups to MG, was bound to Zn(2+) , indicating that GLO I can easily bind to MG. This study provides a structural basis to develop better anticancer drugs. | |||
Crystal structures of human glyoxalase I and its complex with TLSC702 reveal inhibitor binding mode and substrate preference.,Usami M, Ando K, Shibuya A, Takasawa R, Yokoyama H FEBS Lett. 2022 Apr 1. doi: 10.1002/1873-3468.14344. PMID:35363883<ref>PMID:35363883</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7wt0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Lactoylglutathione lyase]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Usami M]] | [[Category: Usami, M]] | ||
[[Category: Yokoyama H]] | [[Category: Yokoyama, H]] | ||
[[Category: Glyoxalase i]] | |||
[[Category: Lyase]] | |||
[[Category: Zinc metalloenzyme]] | |||
Revision as of 10:35, 29 June 2022
human glyoxalase I (with C-ter His tag) in complex with TLSC702human glyoxalase I (with C-ter His tag) in complex with TLSC702
Structural highlights
Function[LGUL_HUMAN] Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B.[1] Publication Abstract from PubMedHuman glyoxalase I (hGLO I) is an enzyme for detoxification of methylglyoxal (MG) and has been considered an attractive target for the development of new anticancer drugs. In our previous report, the GLO I inhibitor TLSC702 induced apoptosis in tumor cells. Here, we determined the crystal structures of hGLO I and its complex with TLSC702. In the complex, the carboxyl O atom of TLSC702 is coordinated to Zn(2+) , and TLSC702 mainly shows van der Waals interaction with hydrophobic residues. In the inhibitor-unbound structure, glycerol, which has similar functional groups to MG, was bound to Zn(2+) , indicating that GLO I can easily bind to MG. This study provides a structural basis to develop better anticancer drugs. Crystal structures of human glyoxalase I and its complex with TLSC702 reveal inhibitor binding mode and substrate preference.,Usami M, Ando K, Shibuya A, Takasawa R, Yokoyama H FEBS Lett. 2022 Apr 1. doi: 10.1002/1873-3468.14344. PMID:35363883[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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