Literature summary 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)
EC Number |
Cloned (Comment) |
Organism |
---|
2.7.2.11 |
Escherichia coli DH5alpha strain proB cloning into pET-22b to yield pGKE, and overexpression |
Escherichia coli |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.7.2.11 |
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
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
2.7.2.11 |
5-oxoproline |
AAK domain has a crater on the beta sheet C-edge that hosts the active centre and binds 5-oxoproline |
Escherichia coli |
|
2.7.2.11 |
L-proline |
AAK domain is responsible for inhibition |
Escherichia coli |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
2.7.2.11 |
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
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.7.2.11 |
Escherichia coli |
P0A7B5 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.7.2.11 |
- |
Escherichia coli |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.7.2.11 |
ATP + L-glutamate |
AAK domain is responsible for catalysis |
Escherichia coli |
ADP + L-glutamate 5-phosphate |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
2.7.2.11 |
tetramer |
crystallographic studies |
Escherichia coli |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.7.2.11 |
G5K |
- |
Escherichia coli |