1gs5
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1gs5.gif|left|200px]] | [[Image:1gs5.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1gs5", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | | | + | --> |
- | | | + | {{STRUCTURE_1gs5| PDB=1gs5 | SCENE= }} |
- | + | ||
- | + | ||
- | }} | + | |
'''N-ACETYL-L-GLUTAMATE KINASE FROM ESCHERICHIA COLI COMPLEXED WITH ITS SUBSTRATE N-ACETYLGLUTAMATE AND ITS SUBSTRATE ANALOG AMPPNP''' | '''N-ACETYL-L-GLUTAMATE KINASE FROM ESCHERICHIA COLI COMPLEXED WITH ITS SUBSTRATE N-ACETYLGLUTAMATE AND ITS SUBSTRATE ANALOG AMPPNP''' | ||
Line 31: | Line 28: | ||
[[Category: Ramon-Maiques, S.]] | [[Category: Ramon-Maiques, S.]] | ||
[[Category: Rubio, V.]] | [[Category: Rubio, V.]] | ||
- | [[Category: | + | [[Category: Acetylglutamate kinase]] |
- | [[Category: | + | [[Category: Amino acid kinase]] |
- | [[Category: | + | [[Category: Arginine biosynthesis]] |
- | [[Category: | + | [[Category: Carbamate kinase]] |
- | [[Category: | + | [[Category: Phosphoryl group transfer]] |
- | [[Category: | + | [[Category: Protein crystallography]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:56:31 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 14:56, 2 May 2008
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. 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 Fri May 2 17:56:31 2008