PDBsum entry: 2ezw

Transferase

PDB id: 2ezw

Contents

Protein chains

50 a.a. *

* Residue conservation analysis

PDB id:

2ezw

Name:

Transferase

Title:

Solution structure of the docking and dimerization domain of the type i alpha regulatory subunit of protein kinase a (rialpha d/d)

Structure:

Camp-dependent protein kinase type i-alpha regulatory subunit. Chain: a, b. Fragment: dimerization-anchoring domain (residues 12-61). Engineered: yes

Source:

Bos taurus. Cattle. Organism_taxid: 9913. Gene: prkar1a (amino acids:12 - 61). Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

18 models

Authors:

P.Banky

Key ref:

P.Banky et al. (2003). Related protein-protein interaction modules present drastically different surface topographies despite a conserved helical platform. J Mol Biol, 330, 1117-1129. PubMed id: 12860132 DOI: 10.1016/S0022-2836(03)00552-7

Date:

10-Nov-05 Release date: 14-Feb-06

Protein chains

P00514  (KAP0_BOVIN) -  cAMP-dependent protein kinase type I-alpha regulatory subunit

Seq: 380 a.a.

Struc: 50 a.a.

 Gene Ontology (GO) functional annotation 

• Biological process: signal transduction (1 term)
• Biochemical function: cAMP-dependent protein kinase regulator activity (1 term)

DOI no: 10.1016/S0022-2836(03)00552-7

J Mol Biol 330:1117-1129 (2003)

PubMed id: 12860132

Related protein-protein interaction modules present drastically different surface topographies despite a conserved helical platform.

P.Banky, M.Roy, M.G.Newlon, D.Morikis, N.M.Haste, S.S.Taylor, P.A.Jennings.

ABSTRACT

The subcellular localization of cAMP-dependent protein kinase (PKA) occurs through interaction with A-Kinase Anchoring Proteins (AKAPs). AKAPs bind to the PKA regulatory subunit dimer of both type Ialpha and type IIalpha (RIalpha and RIIalpha). RIalpha and RIIalpha display characteristic localization within different cell types, which is maintained by interaction of AKAPs with the N-terminal dimerization and docking domain (D/D) of the respective regulatory subunit. Previously, we reported the solution structure of RIIa D/D module, both free and bound to AKAPs. We have now solved the solution structure of the dimerization and docking domain of the type Ialpha regulatory dimer subunit (RIalpha D/D). RIalpha D/D is a compact docking module, with unusual interchain disulfide bonds that help maintain the AKAP interaction surface. In contrast to the shallow hydrophobic groove for AKAP binding across the surface of the RIIalpha D/D dimeric interface, the RIalpha D/D module presents a deep cleft for proposed AKAP binding. RIalpha and RIIalpha D/D interaction modules present drastically differing dimeric topographies, despite a conserved X-type four-helix bundle structure.

Selected figure(s)

Figure 5.
Figure 5. Surface representation of the AKAP binding surface in RIa (12-61) D/D. GRASP rendering of the molecular surface from RIa (12-61) in (A). Residues 12-23 from Helix N-1 and N-1' are in yellow. In (B), the molecule is rotated 45° about the x-axis and highlights the surface exposed cleft on RIa (12-61).

Figure 7.
Figure 7. Sequence alignments of RIa and RIIa D/D domains. From top to bottom, bovine: bRIa (P00514), human: hRIa (P10644), Rattus norvegicus: rRIa (P09456), Sus scrofa: pRIa (P07802), Drosophila melanogaster: DrosRI (P16905), C. elegans: C.E. (P30625), human: hRIb (P31321), rat: rRIb (P81377), M. musculus: mRIb (P12849), R. norvegicus: rRIIa (AAM97689), M. musculus: mRIIa (P12367), D. melanogaster: DroRIIa (AAF86976), strongylocentrotus purpuratus: S.U.RII (Q26619), and bovine: bRIIb (P31322). Sequence computation was performed using the BLAST network service.[63] Hydrophobic residues are colored yellow, polar residues colored green, positively charged residues in blue and acidic residues in red.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2003, 330, 1117-1129) copyright 2003.

Figures were selected by an automated process.