2.7.2.8	-	642361, 642363	
2.7.2.8	as complex with PII protein, NAGK binds Mg2+, ADP, arginine and N-acetylglutamate	674874	
2.7.2.8	crystal structure of Maricaulis maris NAGS/K (mmNAGS/K) at 2.7 A resolution shows that it is a tetramer	720845	
2.7.2.8	crystal structure of the complex between acetylglutamate kinase and PII of Synechococcus elongatus, at 2.75 A resolution	689765	
2.7.2.8	crystal structures of both the DUF619 domain-lacking yNAGK, ligand-free as well as complexed with acetylglutamate or acetylglutamate and arginine, and of complete mature yNAGK are determined. yNAGK has as central structure a flat tetramer formed by two dimers of amino acid kinase domains	723557	
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	hanging drop vapor diffusion method at room temperature, crystal structure of a complex formed between two homotrimers of PII and a single hexamer of enzyme bound to the metabolites N-acetylglutamate, ADP, ATP, and arginine	674874	
2.7.2.8	hanging-drop vapor diffusion method	689895	
2.7.2.8	in complex with arginine	675366	
2.7.2.8	in complex with MgADP-, N-acetyl-glutamte, AlF4-, with MgADP-, N-acetyl-glutamte, with ADp and SO42-	642359	
2.7.2.8	of the recombinant wild type protein, the selenomethionine substituted enzyme, the mutants and the methylated enzyme, cocrystallization with ATP, ADP, acetyl-CoA, CoA, N-acetyl-L-glutamate, adenylylimidodiphosphate, arginine	671144	
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	
2.7.2.8	without arginine	675366