    2.7.2.8 | crystal structures of EcNAGK free from substrates or complexed with the product N-acetyl-L-glutamyl-5-phosphate (NAGP) and with sulfate are determined at 2 A resolution. Structures reveal a novel, very open NAGK conformation to which substrates associate and from which roducts dissociate. In this conformation, the C-domain, which hosts most of the nucleotide site, rotates 24°-28° away from the N-domain, which hosts the acetylglutamate site, whereas the empty ATP site also exhibits some changes |
722965 |
| 2.7.2.8 | purified enzyme in complex with L-arginine, sitting drop vapor diffusion method, mixing of 10 mg/ml protein in 50 mM Tris-HCl, pH 8.0, 50 mM NaCl, 10% glycerol, 5 mM 2-mercaptoethanol, and 1 mM EDTA with 1 mM L-arginine, and 10 mM N-acetyl-L-glutamate for 30 min, 0.002 ml of this protein solution is mixed with 0.002 ml of reservoir solution containing 100 mM sodium cacodylate trihydrate, pH 6.2, 25% PEG P400 and 200 mM magnesium chloride, X-ray diffraction structure determination and analysis at 2.8 A resolution. In contrast to the structure of mmNAGS/K in the absence of L-arginine where there are conformational differences between the four subunits in the asymmetric unit, all four subunits in the L-arginine liganded structure have very similar conformations |
735596 |
