PDBsum entry 3j4q

Transferase

PDB id: 3j4q

Contents

Protein chains

230 a.a.

382 a.a.

325 a.a.

PDB id:

3j4q

Name:

Transferase

Title:

Pseudo-atomic model of the akap18-pka complex in a bent conformation derived from electron microscopy

Structure:

A-kinase anchor protein 18. Chain: a. Fragment: see remark 999. Synonym: akap18. Engineered: yes. Camp-dependent protein kinase type ii-alpha regulatory subunit. Chain: b, c. Synonym: protein kinase, camp dependent regulatory, type ii alpha,

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Mus musculus. Mouse. Organism_taxid: 10090. Gene: prkar2a, mcg_16488.

Authors:

S.L.Reichow,T.Gonen

Key ref:

F.D.Smith et al. (2013). Intrinsic disorder within an AKAP-protein kinase A complex guides local substrate phosphorylation. Elife, 2, e01319. PubMed id: 24192038 DOI: 10.7554/eLife.01319

Date:

25-Sep-13 Release date: 13-Nov-13

Protein chain

Q6JP77  (AKA7G_RAT) -  A-kinase anchor protein 7 isoforms delta and gamma from Rattus norvegicus

Seq: 353 a.a.

Struc: 230 a.a.

Protein chains

P12367  (KAP2_MOUSE) -  cAMP-dependent protein kinase type II-alpha regulatory subunit from Mus musculus

Seq: 401 a.a.

Struc: 382 a.a.*

Protein chains

P05132  (KAPCA_MOUSE) -  cAMP-dependent protein kinase catalytic subunit alpha from Mus musculus

Seq: 351 a.a.

Struc: 325 a.a.

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class 1: Chains A, B, C: E.C.?
• Enzyme class 2: Chains D, E: E.C.2.7.11.11 - cAMP-dependent protein kinase.
• Reaction:
  1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H⁺
  2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H⁺

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.7554/eLife.01319

Elife 2:e01319 (2013)

PubMed id: 24192038

Intrinsic disorder within an AKAP-protein kinase A complex guides local substrate phosphorylation.

F.D.Smith, S.L.Reichow, J.L.Esseltine, D.Shi, L.K.Langeberg, J.D.Scott, T.Gonen.

ABSTRACT

Anchoring proteins sequester kinases with their substrates to locally disseminate intracellular signals and avert indiscriminate transmission of these responses throughout the cell. Mechanistic understanding of this process is hampered by limited structural information on these macromolecular complexes. A-kinase anchoring proteins (AKAPs) spatially constrain phosphorylation by cAMP-dependent protein kinases (PKA). Electron microscopy and three-dimensional reconstructions of type-II PKA-AKAP18γ complexes reveal hetero-pentameric assemblies that adopt a range of flexible tripartite configurations. Intrinsically disordered regions within each PKA regulatory subunit impart the molecular plasticity that affords an ∼16 nanometer radius of motion to the associated catalytic subunits. Manipulating flexibility within the PKA holoenzyme augmented basal and cAMP responsive phosphorylation of AKAP-associated substrates. Cell-based analyses suggest that the catalytic subunit remains within type-II PKA-AKAP18γ complexes upon cAMP elevation. We propose that the dynamic movement of kinase sub-structures, in concert with the static AKAP-regulatory subunit interface, generates a solid-state signaling microenvironment for substrate phosphorylation. DOI: http://dx.doi.org/10.7554/eLife.01319.001.