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4DIN

Novel Localization and Quaternary Structure of the PKA RI beta Holoenzyme

Summary for 4DIN
Entry DOI10.2210/pdb4din/pdb
Related2QCS
DescriptorcAMP-dependent protein kinase catalytic subunit alpha, cAMP-dependent protein kinase type I-beta regulatory subunit, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
Functional Keywordsisoform diversity, rib2:c2 tetrameric complex, transferase-transport protein complex, transferase/transport protein
Biological sourceMus musculus (mouse)
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Cellular locationCytoplasm: P05132
Total number of polymer chains2
Total formula weight84343.99
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 citationIlouz, 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: 22797896
DOI: 10.1073/pnas.1209538109
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.7 Å)
Structure validation

236060

数据于2025-05-14公开中

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