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6PW4

Cryo-EM Structure of Thermo-Sensitive TRP Channel TRP1 from the Alga Chlamydomonas reinhardtii in Detergent

Summary for 6PW4
Entry DOI10.2210/pdb6pw4/pdb
EMDB information20498 20499
DescriptorTRP-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 Keywordsion channels, membrane protein, trp channels, transport protein
Biological sourceChlamydomonas reinhardtii
Total number of polymer chains4
Total formula weight406622.43
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 citationMcGoldrick, 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: 31519888
DOI: 10.1038/s41467-019-12121-9
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.53 Å)
Structure validation

237735

数据于2025-06-18公开中

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