1gs5
From Proteopedia
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| - | [[Image:1gs5.gif|left|200px]] | + | [[Image:1gs5.gif|left|200px]] |
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| - | '''N-ACETYL-L-GLUTAMATE KINASE FROM ESCHERICHIA COLI COMPLEXED WITH ITS SUBSTRATE N-ACETYLGLUTAMATE AND ITS SUBSTRATE ANALOG AMPPNP''' | + | {{Structure |
| + | |PDB= 1gs5 |SIZE=350|CAPTION= <scene name='initialview01'>1gs5</scene>, resolution 1.5Å | ||
| + | |SITE= <scene name='pdbsite=NLG:Mg+Binding+Site+For+Chain+A'>NLG</scene> | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NLG:N-ACETYL-L-GLUTAMATE'>NLG</scene> and <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'>ANP</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''N-ACETYL-L-GLUTAMATE KINASE FROM ESCHERICHIA COLI COMPLEXED WITH ITS SUBSTRATE N-ACETYLGLUTAMATE AND ITS SUBSTRATE ANALOG AMPPNP''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GS5 is a [ | + | 1GS5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GS5 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12005432 12005432] |
[[Category: Acetylglutamate kinase]] | [[Category: Acetylglutamate kinase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: protein crystallography]] | [[Category: protein crystallography]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:27:09 2008'' |
Revision as of 09:27, 20 March 2008
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| , resolution 1.5Å | |||||||
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| Sites: | |||||||
| Ligands: | , and | ||||||
| Activity: | Acetylglutamate kinase, with EC number 2.7.2.8 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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