1gs5
From Proteopedia
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N-ACETYL-L-GLUTAMATE KINASE FROM ESCHERICHIA COLI COMPLEXED WITH ITS SUBSTRATE N-ACETYLGLUTAMATE AND ITS SUBSTRATE ANALOG AMPPNP
Overview
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.
About this Structure
1GS5 is a Single protein structure of sequence from Escherichia coli with MG, NLG and ANP as ligands. Active as Acetylglutamate kinase, with EC number 2.7.2.8 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structure of acetylglutamate kinase, a key enzyme for arginine biosynthesis and a prototype for the amino acid kinase enzyme family, during catalysis., Ramon-Maiques S, Marina A, Gil-Ortiz F, Fita I, Rubio V, Structure. 2002 Mar;10(3):329-42. PMID:12005432
Page seeded by OCA on Tue Dec 18 15:34:03 2007
