 |
PDBsum entry 1smh
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Signaling protein,transferase/inhibitor
|
PDB id
|
|
|
|
1smh
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
The typically disordered n-Terminus of pka can fold as a helix and project the myristoylation site into solution.
|
|
|
Authors
|
|
C.Breitenlechner,
R.A.Engh,
R.Huber,
V.Kinzel,
D.Bossemeyer,
M.Gassel.
|
|
|
Ref.
|
|
Biochemistry, 2004,
43,
7743-7749.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Protein kinases comprise the major enzyme family critically involved in signal
transduction pathways; posttranslational modifications affect their regulation
and determine signaling states. The prototype protein kinase A (PKA) possesses
an N-terminal alpha-helix (Helix A) that is atypical for kinases and is thus a
major distinguishing feature of PKA. Its physiological function may involve
myristoylation at the N-terminus and modulation via phosphorylation at serine
10. Here we describe an unusual structure of an unmyristoylated PKA,
unphosphorylated at serine 10, with a completely ordered N-terminus. Using
standard conditions (e.g., PKI 5-24, ATP site ligand, MEGA-8), a novel 2-fold
phosphorylated PKA variant showed the ordered N-terminus in a new crystal
packing arrangement. Thus, the critical factor for structuring the N-terminus is
apparently the absence of phosphorylation of Ser10. The flexibility of the
N-terminus, its myristoylation, and the conformational dependence on the
phosphorylation state are consistent with a functional role for myristoylation.
|
|
|
|
|
|
|
