4USJ
N-acetylglutamate kinase from Arabidopsis thaliana in complex with PII from Chlamydomonas reinhardtii
Summary for 4USJ
| Entry DOI | 10.2210/pdb4usj/pdb |
| Related | 4USH 4USI |
| Descriptor | ACETYLGLUTAMATE KINASE, CHLOROPLASTIC, NITROGEN REGULATORY PROTEIN PII, ARGININE, ... (10 entities in total) |
| Functional Keywords | transferase, nagk, nitrogen assimilation, q-loop, c-terminal extension, protein-protein complex, regulation of arginine metabolism, signaling protein |
| Biological source | ARABIDOPSIS THALIANA (THALE CRESS) More |
| Cellular location | Plastid, chloroplast stroma : Q9SCL7 |
| Total number of polymer chains | 4 |
| Total formula weight | 103609.93 |
| Authors | Chellamuthu, V.R.,Forchhammer, K.,Hartmann, M.D. (deposition date: 2014-07-08, release date: 2014-12-03, Last modification date: 2024-01-10) |
| Primary citation | Chellamuthu, V.R.,Ermilova, E.,Lapina, T.,Luddecke, J.,Minaeva, E.,Herrmann, C.,Hartmann, M.D.,Forchhammer, K. A Widespread Glutamine-Sensing Mechanism in the Plant Kingdom. Cell(Cambridge,Mass.), 159:1188-, 2014 Cited by PubMed Abstract: Glutamine is the primary metabolite of nitrogen assimilation from inorganic nitrogen sources in microorganisms and plants. The ability to monitor cellular nitrogen status is pivotal for maintaining metabolic homeostasis and sustaining growth. The present study identifies a glutamine-sensing mechanism common in the entire plant kingdom except Brassicaceae. The plastid-localized PII signaling protein controls, in a glutamine-dependent manner, the key enzyme of the ornithine synthesis pathway, N-acetyl-l-glutamate kinase (NAGK), that leads to arginine and polyamine formation. Crystal structures reveal that the plant-specific C-terminal extension of PII, which we term the Q loop, forms a low-affinity glutamine-binding site. Glutamine binding alters PII conformation, promoting interaction and activation of NAGK. The binding motif is highly conserved in plants except Brassicaceae. A functional Q loop restores glutamine sensing in a recombinant Arabidopsis thaliana PII protein, demonstrating the modular concept of the glutamine-sensing mechanism adopted by PII proteins during the evolution of plant chloroplasts. PubMed: 25416954DOI: 10.1016/J.CELL.2014.10.015 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.85 Å) |
Structure validation
Download full validation report
