Structural highlights
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.
See Also
References
- ↑ Kim YJ. A cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase. Acta Crystallogr F Struct Biol Commun. 2018 May 1;74(Pt 5):277-282. doi:, 10.1107/S2053230X18004557. Epub 2018 Apr 16. PMID:29717994 doi:https://dx.doi.org/10.1107/S2053230X18004557
