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Structure paper

TitleThe structures of protein kinase A in complex with CFTR: Mechanisms of phosphorylation and noncatalytic activation.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 121, Issue 46, Page e2409049121, Year 2024
Publish dateNov 12, 2024
AuthorsKarol Fiedorczuk / Iordan Iordanov / Csaba Mihályi / Andras Szollosi / László Csanády / Jue Chen /
PubMed AbstractProtein kinase A (PKA) is a key regulator of cellular functions by selectively phosphorylating numerous substrates, including ion channels, enzymes, and transcription factors. It has long served as a ...Protein kinase A (PKA) is a key regulator of cellular functions by selectively phosphorylating numerous substrates, including ion channels, enzymes, and transcription factors. It has long served as a model system for understanding the eukaryotic kinases. Using cryoelectron microscopy, we present complex structures of the PKA catalytic subunit (PKA-C) bound to a full-length protein substrate, the cystic fibrosis transmembrane conductance regulator (CFTR)-an ion channel vital to human health. CFTR gating requires phosphorylation of its regulatory (R) domain. Unphosphorylated CFTR engages PKA-C at two locations, establishing two "catalytic stations" near to, but not directly involving, the R domain. This configuration, coupled with the conformational flexibility of the R domain, permits transient interactions of the eleven spatially separated phosphorylation sites. Furthermore, we determined two structures of the open-pore CFTR stabilized by PKA-C, providing a molecular basis to understand how PKA-C stimulates CFTR currents even in the absence of phosphorylation.
External linksProc Natl Acad Sci U S A / PubMed:39495916 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 9.0 Å
Structure data

47235

9dw4

EMDB-47235, PDB-9dw4:
Dephosphorylated CFTR in 1:1 complex with PKA-C (site II)
Method: EM (single particle) / Resolution: 9.0 Å

47236

9dw5

EMDB-47236, PDB-9dw5:
Dephosphorylated CFTR in 1:1 complex with PKA-C (site I)
Method: EM (single particle) / Resolution: 3.8 Å

47237

9dw7

EMDB-47237, PDB-9dw7:
Dephosphorylated CFTR in 1:2 complex with PKA-C
Method: EM (single particle) / Resolution: 6.0 Å

47238

9dw8

EMDB-47238, PDB-9dw8:
Dephosphorylated (E1371Q)CFTR in complex with PKA-C
Method: EM (single particle) / Resolution: 3.5 Å

47239

9dw9

EMDB-47239, PDB-9dw9:
Phosphorylated (E1371Q)CFTR in complex with PKA-C
Method: EM (single particle) / Resolution: 2.8 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-B44:
N-(2-phenylethyl)adenosine 5'-(tetrahydrogen triphosphate)

ChemComp-CLR:
CHOLESTEROL

ChemComp-D10:
DECANE

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-CL:
Unknown entry

ChemComp-UND:
UNDECANE

ChemComp-HOH:
WATER

Source
  • bos taurus (domestic cattle)
  • homo sapiens (human)
KeywordsHYDROLASE / CFTR / PKA / complex

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