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TitleStructure of the ancient TRPY1 channel from Saccharomyces cerevisiae reveals mechanisms of modulation by lipids and calcium.
Journal, issue, pagesStructure, Vol. 30, Issue 1, Page 139-155.e5, Year 2022
Publish dateJan 6, 2022
AuthorsTofayel Ahmed / Collin R Nisler / Edwin C Fluck / Sanket Walujkar / Marcos Sotomayor / Vera Y Moiseenkova-Bell /
PubMed AbstractTransient receptor potential (TRP) channels emerged in fungi as mechanosensitive osmoregulators. The Saccharomyces cerevisiae vacuolar TRP yeast 1 (TRPY1) is the most studied TRP channel from fungi, ...Transient receptor potential (TRP) channels emerged in fungi as mechanosensitive osmoregulators. The Saccharomyces cerevisiae vacuolar TRP yeast 1 (TRPY1) is the most studied TRP channel from fungi, but the structure and details of channel modulation remain elusive. Here, we describe the full-length cryoelectron microscopy structure of TRPY1 at 3.1 Å resolution in a closed state. The structure, despite containing an evolutionarily conserved and archetypical transmembrane domain, reveals distinctive structural folds for the cytosolic N and C termini, compared with other eukaryotic TRP channels. We identify an inhibitory phosphatidylinositol 3-phosphate (PI(3)P) lipid-binding site, along with two Ca-binding sites: a cytosolic site, implicated in channel activation and a vacuolar lumen site, implicated in inhibition. These findings, together with data from microsecond-long molecular dynamics simulations and a model of a TRPY1 open state, provide insights into the basis of TRPY1 channel modulation by lipids and Ca, and the molecular evolution of TRP channels.
External linksStructure / PubMed:34453887 / PubMed Central
MethodsEM (single particle)
Resolution3.1 Å
Structure data

21672

6whg

EMDB-21672, PDB-6whg:
PI3P and calcium bound full-length TRPY1 in detergent
Method: EM (single particle) / Resolution: 3.1 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-PWE:
(2R)-1-(butanoyloxy)-3-{[(R)-hydroxy{[(1S,2S,3S,4S,5S,6R)-2,3,4,6-tetrahydroxy-5-(phosphonooxy)cyclohexyl]oxy}phosphoryl]oxy}propan-2-yl hexadecanoate

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsMEMBRANE PROTEIN / Ion channel

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