6WHG
PI3P and calcium bound full-length TRPY1 in detergent
Summary for 6WHG
| Entry DOI | 10.2210/pdb6whg/pdb |
| EMDB information | 21672 |
| Descriptor | Calcium channel YVC1, CALCIUM ION, (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 (3 entities in total) |
| Functional Keywords | ion channel, membrane protein |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Total number of polymer chains | 4 |
| Total formula weight | 315349.80 |
| Authors | Ahmed, T.,Moiseenkova-Bell, V.Y. (deposition date: 2020-04-08, release date: 2021-04-21, Last modification date: 2024-05-29) |
| Primary citation | Ahmed, T.,Nisler, C.R.,Fluck 3rd, E.C.,Walujkar, S.,Sotomayor, M.,Moiseenkova-Bell, V.Y. Structure of the ancient TRPY1 channel from Saccharomyces cerevisiae reveals mechanisms of modulation by lipids and calcium. Structure, 30:139-, 2022 Cited by PubMed Abstract: 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. PubMed: 34453887DOI: 10.1016/j.str.2021.08.003 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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