6PW4
Cryo-EM Structure of Thermo-Sensitive TRP Channel TRP1 from the Alga Chlamydomonas reinhardtii in Detergent
Summary for 6PW4
Entry DOI | 10.2210/pdb6pw4/pdb |
EMDB information | 20498 20499 |
Descriptor | TRP-like ion channel, [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate, 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE, ... (5 entities in total) |
Functional Keywords | ion channels, membrane protein, trp channels, transport protein |
Biological source | Chlamydomonas reinhardtii |
Total number of polymer chains | 4 |
Total formula weight | 406622.43 |
Authors | McGoldrick, L.L.,Singh, A.K.,Sobolevsky, A.I. (deposition date: 2019-07-22, release date: 2019-09-25, Last modification date: 2024-03-20) |
Primary citation | McGoldrick, L.L.,Singh, A.K.,Demirkhanyan, L.,Lin, T.Y.,Casner, R.G.,Zakharian, E.,Sobolevsky, A.I. Structure of the thermo-sensitive TRP channel TRP1 from the alga Chlamydomonas reinhardtii. Nat Commun, 10:4180-4180, 2019 Cited by PubMed Abstract: Algae produce the largest amount of oxygen on earth and are invaluable for human nutrition and biomedicine, as well as for the chemical industry, energy production and agriculture. The mechanisms by which algae can detect and respond to changes in their environments can rely on membrane receptors, including TRP ion channels. Here we present a 3.5-Å resolution cryo-EM structure of the transient receptor potential (TRP) channel crTRP1 from the alga Chlamydomonas reinhardtii that opens in response to increased temperature and is positively regulated by the membrane lipid PIP. The structure of crTRP1 significantly deviates from the structures of other TRP channels and has a unique 2-fold symmetrical rose-shape architecture with elbow domains and ankyrin repeat domains submerged and dipping into the membrane, respectively. Our study provides a structure of a TRP channel from a micro-organism and a structural framework for better understanding algae biology and TRP channel evolution. PubMed: 31519888DOI: 10.1038/s41467-019-12121-9 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.53 Å) |
Structure validation
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