1gs5
From Proteopedia
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==Overview== | ==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, . | + | 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== | ==About this Structure== | ||
| - | 1GS5 is a | + | 1GS5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG, NLG and ANP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acetylglutamate_kinase Acetylglutamate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.8 2.7.2.8] Structure known Active Site: NLG. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GS5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protein crystallography]] | [[Category: protein crystallography]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:16:50 2007'' |
Revision as of 12:11, 5 November 2007
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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 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
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