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Publication Abstract from PubMed

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a glycolytic enzyme, catalyses the conversion of D-glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate. While mammalian and yeast GAPDHs are multifunctional proteins that have additional functions beyond those involved in glycolysis, including reactions related to nuclear RNA transport, DNA replication/repair, membrane fusion and cellular apoptosis, Escherichia coli GAPDH (ecGAPDH) has only been reported to function in glycolysis. The S-loop of GAPDH is required for interaction with its cofactor and with other proteins. In this study, the three-dimensional crystal structure of GAPDH treated with trehalose is reported at 2.0 A resolution. Trehalose was used as a cryoprotectant for the GAPDH crystals. The structure of trehalose-bound ecGAPDH was compared with the structures of both NAD(+)-free and NAD(+)-bound ecGAPDH. At the S-loop, the bound trehalose in the GAPDH structure induces a 2.4 degrees rotation compared with the NAD(+)-free ecGAPDH structure and a 3.1 degrees rotation compared with the NAD(+)-bound ecGAPDH structure.

A cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase.,Kim YJ Acta Crystallogr F Struct Biol Commun. 2018 May 1;74(Pt 5):277-282. doi:, 10.1107/S2053230X18004557. Epub 2018 Apr 16. PMID:29717994^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.