Application | Comment | Organism |
---|---|---|
medicine | GMPK from bacterial pathogens, in which this enzyme is essential, are potential targets for therapeutic inhibition. | Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
vapour diffusion method | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Ap5G | Ap5G locks an incompletely closed conformation of the enzyme, in which the adenine moiety is located outside its expected binding site. Instead, it binds at a subunit interface that is unique to the bacterial enzyme, which is in equilibrium between a dimeric and an hexameric form in solution. | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
dGMP + ATP | Escherichia coli | GMPKs catalyze the reversible phosphorylation of GMP and dGMP to their diphosphate form in the cell using ATP as a preferred phosphate donor. | dGDP + ADP | - |
r | |
GMP + ATP | Escherichia coli | GMPKs catalyze the reversible phosphorylation of GMP and dGMP to their diphosphate form in the cell using ATP as a preferred phosphate donor. | GDP + ADP | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P60546 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
dGMP + ATP | GMPKs catalyze the reversible phosphorylation of GMP and dGMP to their diphosphate form in the cell using ATP as a preferred phosphate donor. | Escherichia coli | dGDP + ADP | - |
r | |
GMP + ATP | GMPKs catalyze the reversible phosphorylation of GMP and dGMP to their diphosphate form in the cell using ATP as a preferred phosphate donor. | Escherichia coli | GDP + ADP | - |
r |
Subunits | Comment | Organism |
---|---|---|
hexamer | X-ray diffraction data for EcGMPK in complex with GCV-MP were collected at 100 K from a single crystal on beamline ID23-1 (lambda = 0.980 A) at the European Synchrotron Radiation Facility (Grenoble, France), and is indexed and scaled using XDS and XSCALE to a resolution of 3.16 A. Crystals of EcGMPK GCV-MP belong to space group P41212 and are isomorphous to those of apo-EcGMPK, with 6 molecules related by D3 symmetry in the asymmetric unit. Each monomer was first divided in 3 domains corresponding to the LID, CORE and GMP-binding domains (except for subunit F whose GMP-binding domain is not visible in apo-EcGMPK), which were submitted to rigid body refinement. | Escherichia coli |
More | GMPKs share a highly conserved structure comprising a GMP-binding domain, a central CORE domain that carries the ATP beta-phosphate binding loop (P-loop) and a LID domain which binds the adenine base of ATP and provides catalytic residues to the phosphoryl transfer reaction. | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
apo-EcGMPK | - |
Escherichia coli |
guanosine monophosphate kinase (EcGMPK) | - |
Escherichia coli |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.0005 | - |
The crystal structure of EcGMPK in complex with Ap5G solved at 2.5 Å resolution. | Escherichia coli | Ap5G |