1GS5

N-acetyl-L-glutamate kinase from Escherichia coli complexed with its substrate N-acetylglutamate and its substrate analog AMPPNP

Summary for 1GS5

• Entry DOI: 10.2210/pdb1gs5/pdb
• Descriptor: ACETYLGLUTAMATE KINASE, N-ACETYL-L-GLUTAMATE, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (5 entities in total)
• Functional Keywords: carbamate kinase, amino acid kinase, arginine biosynthesis, phosphoryl group transfer, transferase
• Biological source: ESCHERICHIA COLI
• Cellular location: Cytoplasm (Probable): P11445
• Total number of polymer chains: 1
• Total formula weight: 27906.16

Authors

Ramon-Maiques, S.,Marina, A.,Gil-Ortiz, F.,Fita, I.,Rubio, V. (deposition date: 2001-12-28, release date: 2002-05-16, Last modification date: 2023-12-13)

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

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: 12005432
DOI: 10.1016/S0969-2126(02)00721-9

Experimental method

X-RAY DIFFRACTION (1.5 Å)