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7wt1
From Proteopedia
(Difference between revisions)
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==human glyoxalase I (with C-ter His tag) in inhibitor-free form== | ==human glyoxalase I (with C-ter His tag) in inhibitor-free form== | ||
| - | <StructureSection load='7wt1' size='340' side='right'caption='[[7wt1]]' scene=''> | + | <StructureSection load='7wt1' size='340' side='right'caption='[[7wt1]], [[Resolution|resolution]] 1.85Å' 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=7WT1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WT1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7wt1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WT1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WT1 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=7wt1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wt1 OCA], [https://pdbe.org/7wt1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wt1 RCSB], [https://www.ebi.ac.uk/pdbsum/7wt1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wt1 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=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=7wt1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wt1 OCA], [https://pdbe.org/7wt1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wt1 RCSB], [https://www.ebi.ac.uk/pdbsum/7wt1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wt1 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 7wt1" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Lactoylglutathione lyase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Shibuya A]] | + | [[Category: Shibuya, A]] |
| - | [[Category: Usami M]] | + | [[Category: Usami, M]] |
| - | [[Category: Yokoyama H]] | + | [[Category: Yokoyama, H]] |
| + | [[Category: Glyoxalase i]] | ||
| + | [[Category: Lyase]] | ||
| + | [[Category: Zinc metalloenzyme]] | ||
Revision as of 07:35, 29 June 2022
human glyoxalase I (with C-ter His tag) in inhibitor-free form
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