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TitleAnionic lipids unlock the gates of select ion channels in the pacemaker family.
Journal, issue, pagesNat Struct Mol Biol, Vol. 29, Issue 11, Page 1092-1100, Year 2022
Publish dateNov 9, 2022
AuthorsPhilipp A M Schmidpeter / Di Wu / Jan Rheinberger / Paul M Riegelhaupt / Haiping Tang / Carol V Robinson / Crina M Nimigean /
PubMed AbstractLipids play important roles in regulating membrane protein function, but the molecular mechanisms used are elusive. Here we investigated how anionic lipids modulate SthK, a bacterial pacemaker ...Lipids play important roles in regulating membrane protein function, but the molecular mechanisms used are elusive. Here we investigated how anionic lipids modulate SthK, a bacterial pacemaker channel homolog, and HCN2, whose activity contributes to pacemaking in the heart and brain. Using SthK allowed the reconstitution of purified channels in controlled lipid compositions for functional and structural assays that are not available for the eukaryotic channels. We identified anionic lipids bound tightly to SthK and their exact binding locations and determined that they potentiate channel activity. Cryo-EM structures in the most potentiating lipids revealed an open state and identified a nonannular lipid bound with its headgroup near an intersubunit salt bridge that clamps the intracellular channel gate shut. Breaking this conserved salt bridge abolished lipid modulation in SthK and eukaryotic HCN2 channels, indicating that anionic membrane lipids facilitate channel opening by destabilizing these interactions. Our findings underline the importance of state-dependent protein-lipid interactions.
External linksNat Struct Mol Biol / PubMed:36352139 / PubMed Central
MethodsEM (single particle)
Resolution2.41 - 3.6 Å
Structure data

25916

7tj5

EMDB-25916, PDB-7tj5:
SthK closed state, cAMP-bound in the presence of POPA
Method: EM (single particle) / Resolution: 2.41 Å

25917

7tj6

EMDB-25917, PDB-7tj6:
SthK open state, cAMP-bound in the presence of POPA
Method: EM (single particle) / Resolution: 2.9 Å

25981

7tkt

EMDB-25981, PDB-7tkt:
SthK closed state, cAMP-bound in the presence of detergent
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

ChemComp-CMP:
ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE / Cyclic adenosine monophosphate

ChemComp-D21:
(2R)-1-(hexadecanoyloxy)-3-(phosphonooxy)propan-2-yl (9Z)-octadec-9-enoate

ChemComp-PGW:
(1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(hexadecanoyloxy)methyl]ethyl / phospholipid*YM / Phosphatidylglycerol

Source
  • Spirochaeta thermophila (strain ATCC 700085 / DSM 6578 / Z-1203) (bacteria)
  • spirochaeta thermophila dsm 6578 (bacteria)
KeywordsTRANSPORT PROTEIN / cyclic nucleotide-gated channel / lipid modulation / pacemaker channel

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