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A cryoprotectant induces conformational change in glyceraldehyde‐3‐phosphate dehydrogenase
Author(s) -
Kim Yong Ju
Publication year - 2018
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x18004557
Subject(s) - glyceraldehyde 3 phosphate dehydrogenase , nad+ kinase , dehydrogenase , biochemistry , trehalose , glyceraldehyde , chemistry , cofactor , biology , enzyme
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 ( ec GAPDH) 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 Å resolution. Trehalose was used as a cryoprotectant for the GAPDH crystals. The structure of trehalose‐bound ec GAPDH was compared with the structures of both NAD + ‐free and NAD + ‐bound ec GAPDH. At the S‐loop, the bound trehalose in the GAPDH structure induces a 2.4° rotation compared with the NAD + ‐free ec GAPDH structure and a 3.1° rotation compared with the NAD + ‐bound ec GAPDH structure.