Unknown

Dataset Information

0

A cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase.


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.

SUBMITTER: Kim YJ 

PROVIDER: S-EPMC5931139 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

A cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase.

Kim Yong Ju YJ  

Acta crystallographica. Section F, Structural biology communications 20180416 Pt 5


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  ...[more]

Similar Datasets

| S-EPMC3549054 | biostudies-literature
| S-EPMC3421169 | biostudies-literature
| S-EPMC3224139 | biostudies-literature
2015-10-30 | E-MTAB-3262 | biostudies-arrayexpress
| S-EPMC5752021 | biostudies-literature
| S-EPMC2242934 | biostudies-literature
| S-EPMC5387080 | biostudies-literature
| S-EPMC2766228 | biostudies-literature
| S-EPMC7281563 | biostudies-literature
| S-EPMC5894109 | biostudies-literature