5ZA0

A cryo-protectant induces the conformational change of glyceraldehyde-3-phosphate dehydrogenase

Summary for 5ZA0

• Entry DOI: 10.2210/pdb5za0/pdb
• Related PRD ID: PRD_900006
• Descriptor: Glyceraldehyde-3-phosphate dehydrogenase A, alpha-D-glucopyranose-(1-1)-alpha-D-glucopyranose, SULFATE ION, ... (4 entities in total)
• Functional Keywords: hypothetical, oxidoreductase, cryo-protectant, glycolysis
• Biological source: Escherichia coli K-12
• Cellular location: Cytoplasm : P0A9B2
• Total number of polymer chains: 1
• Total formula weight: 36015.79

Authors

Kim, Y.J. (deposition date: 2018-02-06, release date: 2018-05-30, Last modification date: 2023-11-22)

Primary citation

Kim, Y.J.
A cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase.
Acta Crystallogr F Struct Biol Commun, 74:277-282, 2018

PubMed Abstract: 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 Å 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° rotation compared with the NAD-free ecGAPDH structure and a 3.1° rotation compared with the NAD-bound ecGAPDH structure.

PubMed: 29717994
DOI: 10.1107/S2053230X18004557

Experimental method

X-RAY DIFFRACTION (2 Å)