4Z0H

X-ray structure of cytoplasmic glyceraldehyde-3-phosphate dehydrogenase (GapC1) complexed with NAD

4Z0H の概要

• エントリーDOI: 10.2210/pdb4z0h/pdb
• 関連するPDBエントリー: 3K2B
• 分子名称: Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolic, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: cytoplasm, glycolysis, rossmann fold, nad complex, oxidoreductase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• 細胞内の位置: Cytoplasm: P25858
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 75034.71

構造登録者

Fermani, S.,Zaffagnini, M.,Orru, R.,Falini, G.,Trost, P. (登録日: 2015-03-26, 公開日: 2016-04-13, 最終更新日: 2024-01-10)

主引用文献

Zaffagnini, M.,Fermani, S.,Calvaresi, M.,Orru, R.,Iommarini, L.,Sparla, F.,Falini, G.,Bottoni, A.,Trost, P.
Tuning Cysteine Reactivity and Sulfenic Acid Stability by Protein Microenvironment in Glyceraldehyde-3-Phosphate Dehydrogenases of Arabidopsis thaliana.
Antioxid. Redox Signal., 24:502-517, 2016

PubMed Abstract: Cysteines and H2O2 are fundamental players in redox signaling. Cysteine thiol deprotonation favors the reaction with H2O2 that generates sulfenic acids with dual electrophilic/nucleophilic nature. The protein microenvironment surrounding the target cysteine is believed to control whether sulfenic acid can be reversibly regulated by disulfide formation or irreversibly oxidized to sulfinates/sulfonates. In this study, we present experimental oxidation kinetics and a quantum mechanical/molecular mechanical (QM/MM) investigation to elucidate the reaction of H2O2 with glycolytic and photosynthetic glyceraldehyde-3-phosphate dehydrogenase from Arabidopsis thaliana (cytoplasmic AtGAPC1 and chloroplastic AtGAPA, respectively).

PubMed: 26650776
DOI: 10.1089/ars.2015.6417

実験手法

X-RAY DIFFRACTION (2.3 Å)