6YNE

GAPDH purified from the supernatant of HEK293F cells: crystal form 2 of 4.

6YNE の概要

• エントリーDOI: 10.2210/pdb6yne/pdb
• 関連するPDBエントリー: 6YND 6YNF 6YNH
• 分子名称: Glyceraldehyde-3-phosphate dehydrogenase, 3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL (3 entities in total)
• 機能のキーワード: hek293f, kifunensine, biosynthetic protein
• 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: 150357.70

構造登録者

Roversi, P.,Lia, A. (登録日: 2020-04-13, 公開日: 2020-05-06, 最終更新日: 2024-01-24)

主引用文献

Lia, A.,Dowle, A.,Taylor, C.,Santino, A.,Roversi, P.
Partial catalytic Cys oxidation of human GAPDH to Cys-sulfonic acid.
Wellcome Open Res, 5:114-114, 2020

PubMed Abstract: : n-Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) catalyses the NAD -dependent oxidative phosphorylation of n-glyceraldehyde-3-phosphate to 1,3-diphospho-n-glycerate and its reverse reaction in glycolysis and gluconeogenesis. : Four distinct crystal structures of human n-Glyceraldehyde-3-phosphate dehydrogenase ( GAPDH) have been determined from protein purified from the supernatant of HEK293F human epithelial kidney cells. : X-ray crystallography and mass-spectrometry indicate that the catalytic cysteine of the protein ( GAPDH Cys152) is partially oxidised to cysteine S-sulfonic acid. The average occupancy for the Cys152-S-sulfonic acid modification over the 20 crystallographically independent copies of GAPDH across three of the crystal forms obtained is 0.31±0.17. : The modification induces no significant structural changes on the tetrameric enzyme, and only makes aspecific contacts to surface residues in the active site, in keeping with the hypothesis that the oxidising conditions of the secreted mammalian cell expression system result in GAPDH catalytic cysteine S-sulfonic acid modification and irreversible inactivation of the enzyme.

PubMed: 32802964
DOI: 10.12688/wellcomeopenres.15893.2

実験手法

X-RAY DIFFRACTION (1.853 Å)