Literature summary for 2.7.2.11 extracted from

Marco-Marin, C.; Gil-Ortiz, F.; Perez-Arellano, I.; Cervera, J.; Fita, I.; Rubio, V.
A novel two-domain architecture within the amino acid kinase enzyme family revealed by the crystal structure of Escherichia coli glutamate 5-kinase (2007), J. Mol. Biol., 367, 1431-1446.

Cloned(Commentary)

Cloned (Comment)	Organism
Escherichia coli DH5alpha strain proB cloning into pET-22b to yield pGKE, and overexpression	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
in about 4-5 months, using the hanging drop vapour diffusion method, complexed with glutamate and sulfate, or with L-glutamate 5-phosphate, sulfate and 5-oxoproline, at 2.9 A and 2.5 A resolution, belongs to the space groups P41212 or P21, respectively. Dimer of dimers architecture, each subunit contains a 257 residue AAK domain, typical of acylphosphate-forming enzymes, with characteristic alpha3beta8alpha4 sandwich topology, each subunit contains a 93 residue C-terminal PUA domain, typical of RNA-modifying enzymes, which presents the characteristic beta5beta4 sandwich fold and three alpha helices	Escherichia coli

Crystallization (Comment)

Organism

in about 4-5 months, using the hanging drop vapour diffusion method, complexed with glutamate and sulfate, or with L-glutamate 5-phosphate, sulfate and 5-oxoproline, at 2.9 A and 2.5 A resolution, belongs to the space groups P41212 or P21, respectively. Dimer of dimers architecture, each subunit contains a 257 residue AAK domain, typical of acylphosphate-forming enzymes, with characteristic alpha3beta8alpha4 sandwich topology, each subunit contains a 93 residue C-terminal PUA domain, typical of RNA-modifying enzymes, which presents the characteristic beta5beta4 sandwich fold and three alpha helices

Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
5-oxoproline	AAK domain has a crater on the beta sheet C-edge that hosts the active centre and binds 5-oxoproline	Escherichia coli
L-proline	AAK domain is responsible for inhibition	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	the AAK and PUA domains of one subunit associate non-canonically in the dimer with the same domains of the other subunit, leaving a negatively charged hole between them that hosts two Mg ions in one crystal, in line with the G5K requirement for free Mg	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A7B5	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-glutamate	AAK domain is responsible for catalysis	Escherichia coli	ADP + L-glutamate 5-phosphate	-	?

Subunits

Subunits	Comment	Organism
tetramer	crystallographic studies	Escherichia coli

Synonyms

Synonyms	Comment	Organism
G5K	-	Escherichia coli