7WT1

human glyoxalase I (with C-ter His tag) in inhibitor-free form

Summary for 7WT1

• Entry DOI: 10.2210/pdb7wt1/pdb
• Descriptor: Lactoylglutathione lyase, ZINC ION (3 entities in total)
• Functional Keywords: glyoxalase i, zinc metalloenzyme, lyase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 43880.56

Authors

Usami, M.,Shibuya, A.,Yokoyama, H. (deposition date: 2022-02-03, release date: 2022-04-13, Last modification date: 2023-11-29)

Primary citation

Usami, M.,Ando, K.,Shibuya, A.,Takasawa, R.,Yokoyama, H.
Crystal structures of human glyoxalase I and its complex with TLSC702 reveal inhibitor binding mode and substrate preference.
Febs Lett., 596:1458-1467, 2022

PubMed Abstract: 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 , 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 , indicating that GLO I can easily bind to MG. This study provides a structural basis to develop better anticancer drugs.

PubMed: 35363883
DOI: 10.1002/1873-3468.14344

Experimental method

X-RAY DIFFRACTION (1.85 Å)