1gs5
From Proteopedia
|
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, ... [(full description)]
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]. Structure known Active Site: NLG. 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 Oct 30 15:18:03 2007
