Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.11.12 extracted from

  • Osborne, B.W.; Wu, J.; McFarland, C.J.; Nickl, C.K.; Sankaran, B.; Casteel, D.E.; Woods, V.L.; Kornev, A.P.; Taylor, S.S.; Dostmann, W.R.
    Crystal structure of cGMP-dependent protein kinase reveals novel site of interchain communication (2011), Structure, 19, 1317-1327.
    View publication on PubMedView publication on EuropePMC

Activating Compound

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(Commentary)

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 (Commentary)

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

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

Organism UniProt Comment Textmining
Bos taurus P00516
-
-

Purification (Commentary)

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

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

Synonyms Comment Organism
PKG
-
Bos taurus
PKGIalpha
-
Bos taurus

General Information

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