7ZVE
K403 acetylated glucose-6-phosphate dehydrogenase (G6PD)
Summary for 7ZVE
| Entry DOI | 10.2210/pdb7zve/pdb |
| Descriptor | Glucose-6-phosphate 1-dehydrogenase, GLYCEROL, COPPER (II) ION, ... (10 entities in total) |
| Functional Keywords | lysine acetylation, metabolic regulation, post-translational modification, genetic code expansion, oxidoreductase |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 8 |
| Total formula weight | 459969.95 |
| Authors | Wu, F.,Muskat, N.H.,Shahar, A.,Arbely, E. (deposition date: 2022-05-15, release date: 2023-08-23, Last modification date: 2024-11-20) |
| Primary citation | Wu, F.,Muskat, N.H.,Dvilansky, I.,Koren, O.,Shahar, A.,Gazit, R.,Elia, N.,Arbely, E. Acetylation-dependent coupling between G6PD activity and apoptotic signaling. Nat Commun, 14:6208-6208, 2023 Cited by PubMed Abstract: Lysine acetylation has been discovered in thousands of non-histone human proteins, including most metabolic enzymes. Deciphering the functions of acetylation is key to understanding how metabolic cues mediate metabolic enzyme regulation and cellular signaling. Glucose-6-phosphate dehydrogenase (G6PD), the rate-limiting enzyme in the pentose phosphate pathway, is acetylated on multiple lysine residues. Using site-specifically acetylated G6PD, we show that acetylation can activate (AcK89) and inhibit (AcK403) G6PD. Acetylation-dependent inactivation is explained by structural studies showing distortion of the dimeric structure and active site of G6PD. We provide evidence for acetylation-dependent K95/97 ubiquitylation of G6PD and Y503 phosphorylation, as well as interaction with p53 and induction of early apoptotic events. Notably, we found that the acetylation of a single lysine residue coordinates diverse acetylation-dependent processes. Our data provide an example of the complex roles of acetylation as a posttranslational modification that orchestrates the regulation of enzymatic activity, posttranslational modifications, and apoptotic signaling. PubMed: 37798264DOI: 10.1038/s41467-023-41895-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.28 Å) |
Structure validation
Download full validation report
