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TitleA conserved mechanism couples cytosolic domain movements to pore gating in the TRPM2 channel.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 121, Issue 46, Page e2415548121, Year 2024
Publish dateNov 12, 2024
AuthorsBalázs Tóth / Yuefeng Jiang / Andras Szollosi / Zhe Zhang / László Csanády /
PubMed AbstractTransient Receptor Potential Melastatin 2 (TRPM2) cation channels contribute to immunocyte activation, insulin secretion, and central thermoregulation. TRPM2 opens upon binding cytosolic Ca and ADP ...Transient Receptor Potential Melastatin 2 (TRPM2) cation channels contribute to immunocyte activation, insulin secretion, and central thermoregulation. TRPM2 opens upon binding cytosolic Ca and ADP ribose (ADPR). We present here the 2.5 Å cryo-electronmicroscopy structure of TRPM2 from (nvTRPM2) in a lipid nanodisc, complexed with Ca and ADPR-2'-phosphate. Comparison with nvTRPM2 without nucleotide reveals that nucleotide binding-induced movements in the protein's three "core" layers deconvolve into a set of rigid-body rotations conserved from cnidarians to man. By covalently crosslinking engineered cysteine pairs we systematically trap the cytosolic layers in specific conformations and study effects on gate opening/closure. The data show that nucleotide binding in Layer 3 disrupts inhibitory intersubunit interactions, allowing rotation of Layer 2 which in turn expands the gate located in Layer 1. Channels trapped in that "activated" state are no longer nucleotide dependent, but are opened by binding of Ca alone.
External linksProc Natl Acad Sci U S A / PubMed:39514307 / PubMed Central
MethodsEM (single particle)
Resolution2.52 - 2.65 Å
Structure data

61524

9jje

EMDB-61524, PDB-9jje:
Nematostella vectensis TRPM2 tetramer in complex with ADPRP/Ca2+
Method: EM (single particle) / Resolution: 2.52 Å

61525

9jjf

EMDB-61525, PDB-9jjf:
Nematostella vectensis TRPM2 protomer in complex with ADPRP/Ca2+
Method: EM (single particle) / Resolution: 2.65 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-A2R:
[(2R,3R,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-3-HYDROXY-4-(PHOSPHONOOXY)TETRAHYDROFURAN-2-YL]METHYL [(2R,3S,4R,5R)-3,4,5-TRIHYDROXYTETRAHYDROFURAN-2-YL]METHYL DIHYDROGEN DIPHOSPHATE

Source
  • nematostella vectensis (starlet sea anemone)
KeywordsMEMBRANE PROTEIN / Nematostella vectensis / TRPM2 / ADPRP / Ca2+

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