4DIN
Novel Localization and Quaternary Structure of the PKA RI beta Holoenzyme
Summary for 4DIN
Entry DOI | 10.2210/pdb4din/pdb |
Related | 2QCS |
Descriptor | cAMP-dependent protein kinase catalytic subunit alpha, cAMP-dependent protein kinase type I-beta regulatory subunit, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total) |
Functional Keywords | isoform diversity, rib2:c2 tetrameric complex, transferase-transport protein complex, transferase/transport protein |
Biological source | Mus musculus (mouse) More |
Cellular location | Cytoplasm: P05132 |
Total number of polymer chains | 2 |
Total formula weight | 84343.99 |
Authors | Ilouz, R.,Bubis, J.,Wu, J.,Yim, Y.Y.,Deal, M.S.,Kornev, A.P.,Ma, Y.,Blumenthal, D.K.,Taylor, S.S. (deposition date: 2012-01-31, release date: 2012-07-04, Last modification date: 2024-10-30) |
Primary citation | Ilouz, R.,Bubis, J.,Wu, J.,Yim, Y.Y.,Deal, M.S.,Kornev, A.P.,Ma, Y.,Blumenthal, D.K.,Taylor, S.S. Localization and quaternary structure of the PKA RI Beta holoenzyme Proc.Natl.Acad.Sci.USA, 109:12443-12448, 2012 Cited by PubMed Abstract: Specificity for signaling by cAMP-dependent protein kinase (PKA) is achieved by both targeting and isoform diversity. The inactive PKA holoenzyme has two catalytic (C) subunits and a regulatory (R) subunit dimer (R(2):C(2)). Although the RIα, RIIα, and RIIβ isoforms are well studied, little is known about RIβ. We show here that RIβ is enriched selectively in mitochondria and hypothesized that its unique biological importance and functional nonredundancy will correlate with its structure. Small-angle X-ray scattering showed that the overall shape of RIβ(2):C(2) is different from its closest homolog, RIα(2):C(2). The full-length RIβ(2):C(2) crystal structure allows us to visualize all the domains of the PKA holoenzyme complex and shows how isoform-specific assembly of holoenzyme complexes can create distinct quaternary structures even though the R(1):C(1) heterodimers are similar in all isoforms. The creation of discrete isoform-specific PKA holoenzyme signaling "foci" paves the way for exploring further biological roles of PKA RIβ and establishes a paradigm for PKA signaling. PubMed: 22797896DOI: 10.1073/pnas.1209538109 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.7 Å) |
Structure validation
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