5ZA0

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

5ZA0 の概要

• エントリーDOI: 10.2210/pdb5za0/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900006
• 分子名称: Glyceraldehyde-3-phosphate dehydrogenase A, alpha-D-glucopyranose-(1-1)-alpha-D-glucopyranose, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: hypothetical, oxidoreductase, cryo-protectant, glycolysis
• 由来する生物種: Escherichia coli K-12
• 細胞内の位置: Cytoplasm : P0A9B2
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36015.79

構造登録者

Kim, Y.J. (登録日: 2018-02-06, 公開日: 2018-05-30, 最終更新日: 2023-11-22)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)