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TitleCryo-EM Visualization of an Active High Open Probability CFTR Anion Channel.
Journal, issue, pagesBiochemistry, Vol. 57, Issue 43, Page 6234-6246, Year 2018
Publish dateOct 30, 2018
AuthorsJonathan F Fay / Luba A Aleksandrov / Timothy J Jensen / Liying L Cui / Joseph N Kousouros / Lihua He / Andrei A Aleksandrov / Drew S Gingerich / John R Riordan / James Z Chen /
PubMed AbstractThe cystic fibrosis transmembrane conductance regulator (CFTR) anion channel, crucial to epithelial salt and water homeostasis, and defective due to mutations in its gene in patients with cystic ...The cystic fibrosis transmembrane conductance regulator (CFTR) anion channel, crucial to epithelial salt and water homeostasis, and defective due to mutations in its gene in patients with cystic fibrosis, is a unique member of the large family of ATP-binding cassette transport proteins. Regulation of CFTR channel activity is stringently controlled by phosphorylation and nucleotide binding. Structural changes that underlie transitions between active and inactive functional states are not yet fully understood. Indeed the first 3D structures of dephosphorylated, ATP-free, and phosphorylated ATP-bound states were only recently reported. Here we have determined the structure of inactive and active states of a thermally stabilized CFTR, the latter with a very high channel open probability, confirmed after reconstitution into proteoliposomes. These structures, obtained at nominal resolution of 4.3 and 6.6 Å, reveal a unique repositioning of the transmembrane helices and regulatory domain density that provide insights into the structural transition between active and inactive functional states of CFTR. Moreover, we observe an extracellular vestibule that may provide anion access to the pore due to the conformation of transmembrane helices 7 and 8 that differs from the previous orthologue CFTR structures. In conclusion, our work contributes detailed structural information on an active, open state of the CFTR anion channel.
External linksBiochemistry / PubMed:30281975
MethodsEM (single particle)
Resolution4.3 - 6.6 Å
Structure data

7793

6d3r

EMDB-7793, PDB-6d3r:
Thermostablilized dephosphorylated chicken CFTR
Method: EM (single particle) / Resolution: 4.3 Å

7794

6d3s

EMDB-7794, PDB-6d3s:
Thermostabilized phosphorylated chicken CFTR
Method: EM (single particle) / Resolution: 6.6 Å

Chemicals

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

Source
  • gallus gallus (chicken)
KeywordsMEMBRANE PROTEIN / CFTR

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