1GSJ
Selenomethionine substituted N-acetyl-L-glutamate kinase from Escherichia coli complexed with its substrate n-acetyl-L-glutamate and its substrate analog AMPPNP
Summary for 1GSJ
| Entry DOI | 10.2210/pdb1gsj/pdb |
| Related | 1GS5 1GSJ |
| Descriptor | ACETYLGLUTAMATE KINASE, N-ACETYL-L-GLUTAMATE, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (5 entities in total) |
| Functional Keywords | kinase, acetylglutamate kinase, selenomethionine, carbamate kinase, amino acid kinase, arginine biosynthesis, phosphoryl group transfer, protein crystallography |
| Biological source | ESCHERICHIA COLI BL21(DE3) |
| Total number of polymer chains | 1 |
| Total formula weight | 28281.32 |
| Authors | Ramon-Maiques, S.,Marina, A.,Gil-Ortiz, F.,Fita, I.,Rubio, V. (deposition date: 2002-01-07, release date: 2002-05-16, Last modification date: 2024-11-13) |
| Primary citation | Ramon-Maiques, S.,Marina, A.,Gil-Ortiz, F.,Fita, I.,Rubio, V. Structure of Acetylglutamate Kinase, a Key Enzyme for Arginine Biosynthesis and a Prototype for the Amino Acid Kinase Enzyme Family, During Catalysis Structure, 10:329-, 2002 Cited by PubMed Abstract: N-Acetyl-L-glutamate kinase (NAGK), a member of the amino acid kinase family, catalyzes the second and frequently controlling step of arginine synthesis. The Escherichia coli NAGK crystal structure to 1.5 A resolution reveals a 258-residue subunit homodimer nucleated by a central 16-stranded molecular open beta sheet sandwiched between alpha helices. In each subunit, AMPPNP, as an alphabetagamma-phosphate-Mg2+ complex, binds along the sheet C edge, and N-acetyl-L-glutamate binds near the dyadic axis with its gamma-COO- aligned at short distance from the gamma-phosphoryl, indicating associative phosphoryl transfer assisted by: (1) Mg2+ complexation; (2) the positive charges on Lys8, Lys217, and on two helix dipoles; and (3) by hydrogen bonding with the y-phosphate. The structural resemblance with carbamate kinase and the alignment of the sequences suggest that NAGK is a structural and functional prototype for the amino acid kinase family, which differs from other acylphosphate-making devices represented by phosphoglycerate kinase, acetate kinase, and biotin carboxylase. PubMed: 12005432DOI: 10.1016/S0969-2126(02)00721-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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