Activating Compound | Comment | Organism | Structure |
---|---|---|---|
cGMP | large conformational changes accompany cGMP binding to the enzyme. A distinct and segregated architecture with an extended central helix separates the two cGMPbinding domains. Additionally, a helical domain (switch helix) promotes the formation of a hydrophobic interface between protomers | Bos taurus |
Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant PKG Ialpha in HEK-293 cells, expression of N-terminally His6-tagged enzyme fragments PKG78-326, PKG78-341,and PKG78-355 in Escherichia coli strain BL21 | Bos taurus |
Crystallization (Comment) | Organism |
---|---|
a recombinant regulatory domain construct, comprising amino acid residues 78-355, containing both cGMP binding sites of PKGIalpha, hanging drop vapor diffusion, from 2.2 M (NH4)2SO4, 100 mM Tris, pH 8.0, 0.2% MPD at a protein concentration of 25-35 mg/ml at 20°C, X-ray diffraction structure determination and analysis at 2.5 A resolution | Bos taurus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of enzyme fragments PKG78-326, PKG78-341, and PKG78-355. Mutational disruption of the Knob-Nest interface in full-length PKG Ia decreases the activation constant and suggests a tethering mechanism for the catalytic domain | Bos taurus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bos taurus | P00516 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant N-terminally His6-tagged enzyme fragments PKG78-326, PKG78-341,and PKG78-355 by nickel affinity chromatography and gel filtration | Bos taurus |
Subunits | Comment | Organism |
---|---|---|
homodimer | the switch helix is a critical site of dimer communication in PKG biology, PKG Ialpha domain organization and general architecture of PKG78-355, overview. PKG maintains both its regulatory and catalytic elements on the same polypeptide chain | Bos taurus |
More | switch helix-mediated dimer interface and modeling of PKG78-355 protomers, overview | Bos taurus |
Synonyms | Comment | Organism |
---|---|---|
PKG | - |
Bos taurus |
PKGIalpha | - |
Bos taurus |
General Information | Comment | Organism |
---|---|---|
evolution | PKG maintains both its regulatory and catalytic elements on the same polypeptide chain.in contrast to PKA, EC 2.7.11.11 | Bos taurus |
additional information | docking studies with enzyme fragments PKG78-326, PKG78-341, and PKG78-355, a Cys117-Cys195 disulfide bond locks A and B helices in the A-domain and is involved in the metal-induced activation of PKG Ialpha, overview | Bos taurus |
physiological function | cGMP-dependent protein kinase serves as an integral component of second messenger signaling in a number of biological contexts including cell differentiation, memory, and vasodilation | Bos taurus |