2RD5
Structural basis for the regulation of N-acetylglutamate kinase by PII in Arabidopsis thaliana
Summary for 2RD5
| Entry DOI | 10.2210/pdb2rd5/pdb |
| Related | 2O66 2O67 |
| Descriptor | Acetylglutamate kinase-like protein, PII protein, ARGININE, ... (8 entities in total) |
| Functional Keywords | protein-protein complex, regulation of arginine biosynthesis, nitrogen metabolism, kinase, transferase, transcription, transcription regulation, protein binding |
| Biological source | Arabidopsis thaliana (thale cress) More |
| Cellular location | Plastid, chloroplast stroma : Q9SCL7 Plastid, chloroplast : Q9ZST4 |
| Total number of polymer chains | 4 |
| Total formula weight | 94738.65 |
| Authors | Mizuno, Y.,Moorhead, G.B.G.,Ng, K.K.S. (deposition date: 2007-09-21, release date: 2007-10-02, Last modification date: 2023-08-30) |
| Primary citation | Mizuno, Y.,Moorhead, G.B.,Ng, K.K. Structural Basis for the Regulation of N-Acetylglutamate Kinase by PII in Arabidopsis thaliana. J.Biol.Chem., 282:35733-35740, 2007 Cited by PubMed Abstract: PII is a highly conserved regulatory protein found in organisms across the three domains of life. In cyanobacteria and plants, PII relieves the feedback inhibition of the rate-limiting step in arginine biosynthesis catalyzed by N-acetylglutamate kinase (NAGK). To understand the molecular structural basis of enzyme regulation by PII, we have determined a 2.5-A resolution crystal structure of a complex formed between two homotrimers of PII and a single hexamer of NAGK from Arabidopsis thaliana bound to the metabolites N-acetylglutamate, ADP, ATP, and arginine. In PII, the T-loop and Trp(22) at the start of the alpha1-helix, which are both adjacent to the ATP-binding site of PII, contact two beta-strands as well as the ends of two central helices (alphaE and alphaG) in NAGK, the opposing ends of which form major portions of the ATP and N-acetylglutamate substrate-binding sites. The binding of Mg(2+).ATP to PII stabilizes a conformation of the T-loop that favors interactions with both open and closed conformations of NAGK. Interactions between PII and NAGK appear to limit the degree of opening and closing of the active-site cleft in opposition to a domain-separating inhibitory effect exerted by arginine, thus explaining the stimulatory effect of PII on the kinetics of arginine-inhibited NAGK. PubMed: 17913711DOI: 10.1074/jbc.M707127200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.51 Å) |
Structure validation
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