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TitleCryo-EM analysis of scorpion toxin binding to Ryanodine Receptors reveals subconductance that is abolished by PKA phosphorylation.
Journal, issue, pagesSci Adv, Vol. 9, Issue 21, Page eadf4936, Year 2023
Publish dateMay 24, 2023
AuthorsOmid Haji-Ghassemi / Yu Seby Chen / Kellie Woll / Georgina B Gurrola / Carmen R Valdivia / Wenxuan Cai / Songhua Li / Hector H Valdivia / Filip Van Petegem /
PubMed AbstractCalcins are peptides from scorpion venom with the unique ability to cross cell membranes, gaining access to intracellular targets. Ryanodine Receptors (RyR) are intracellular ion channels that ...Calcins are peptides from scorpion venom with the unique ability to cross cell membranes, gaining access to intracellular targets. Ryanodine Receptors (RyR) are intracellular ion channels that control release of Ca from the endoplasmic and sarcoplasmic reticulum. Calcins target RyRs and induce long-lived subconductance states, whereby single-channel currents are decreased. We used cryo-electron microscopy to reveal the binding and structural effects of imperacalcin, showing that it opens the channel pore and causes large asymmetry throughout the cytosolic assembly of the tetrameric RyR. This also creates multiple extended ion conduction pathways beyond the transmembrane region, resulting in subconductance. Phosphorylation of imperacalcin by protein kinase A prevents its binding to RyR through direct steric hindrance, showing how posttranslational modifications made by the host organism can determine the fate of a natural toxin. The structure provides a direct template for developing calcin analogs that result in full channel block, with potential to treat RyR-related disorders.
External linksSci Adv / PubMed:37224245 / PubMed Central
MethodsEM (single particle)
Resolution2.84 - 3.84 Å
Structure data

27680

8drp

EMDB-27680, PDB-8drp:
Focus/local refined map in C4 of signal subtracted RyR1 particles
Method: EM (single particle) / Resolution: 2.84 Å

27695

8dtb

EMDB-27695, PDB-8dtb:
Focus/local refined map in C1 of signal subtracted RyR1 particles in complex with ImperaCalcin
Method: EM (single particle) / Resolution: 3.14 Å

27721

8duj

EMDB-27721, PDB-8duj:
Global map in C1 of RyR1 particles in complex with ImperaCalcin
Method: EM (single particle) / Resolution: 3.7 Å

27736

8dve

EMDB-27736, PDB-8dve:
RyR1 in presence of IpCa-T26E phosphomimetic and activating ligands
Method: EM (single particle) / Resolution: 3.84 Å

Chemicals

ChemComp-CFF:
CAFFEINE / medication*YM / Caffeine (data page)

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

ChemComp-ZN:
Unknown entry

ChemComp-CA:
Unknown entry

Source
  • oryctolagus cuniculus (rabbit)
  • pandinus imperator (emperor scorpion)
  • homo sapiens (human)
  • rabbit (rabbit)
KeywordsMEMBRANE PROTEIN / Ryanodine receptor / Ion channel / Snake toxin / Calcin / Complex / TOXIN

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