8P5F

Human wild-type GAPDH,orthorhombic form

これはPDB形式変換不可エントリーです。

8P5F の概要

• エントリーDOI: 10.2210/pdb8p5f/pdb
• 分子名称: Glyceraldehyde-3-phosphate dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ZINC ION, ... (5 entities in total)
• 機能のキーワード: glycolytic, rossman fold, nad-binding, oxidoreductase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 147368.22

構造登録者

Samygina, V.R.,Muronetz, V.I.,Schmalhausen, E.V. (登録日: 2023-05-24, 公開日: 2023-07-05, 最終更新日: 2024-11-06)

主引用文献

Medvedeva, M.V.,Kleimenov, S.Y.,Samygina, V.R.,Muronetz, V.I.,Schmalhausen, E.V.
S-nitrosylation and S-glutathionylation of GAPDH: Similarities, differences, and relationships.
Biochim Biophys Acta Gen Subj, 1867:130418-130418, 2023

PubMed Abstract: The aim of this work was to compare the effect of reversible post-translational modifications, S-nitrosylation and S-glutathionylation, on the properties of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and to reveal the mechanism of the relationship between these modifications. Comparison of S-nitrosylated and S-glutathionylated GAPDH showed that both modifications inactivate the enzyme and change its spatial structure, decreasing the thermal stability of the protein and increasing its sensitivity to trypsin cleavage. Both modifications are reversible in the presence of dithiothreitol, however, in the presence of reduced glutathione and glutaredoxin 1, the reactivation of S-glutathionylated GAPDH is much slower (10% in 2 h) compared to S-nitrosylated GAPDH (60% in 10 min). This suggests that S-glutathionylation is a much less reversible modification compared to S-nitrosylation. Incubation of HEK 293 T cells in the presence of HO or with the NO donor diethylamine NONOate results in accumulation of sulfenated GAPDH (by data of Western blotting) and S-glutathionylated GAPDH (by data of immunoprecipitation with anti-GSH antibodies). Besides GAPDH, a protein of 45 kDa was found to be sulfenated and S-glutathionylated in the cells treated with HO or NO. This protein was identified as beta-actin. The results of this study confirm the previously proposed hypothesis based on in vitro investigations, according to which S-nitrosylation of the catalytic cysteine residue (Cys152) of GAPDH with subsequent formation of cysteine sulfenic acid at Cys152 may promote its S-glutathionylation in the presence of cellular GSH. Presumably, the mechanism may be valid in the case of beta-actin.

PubMed: 37355052
DOI: 10.1016/j.bbagen.2023.130418

実験手法

X-RAY DIFFRACTION (1.82 Å)