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Nat Commun. 2019 Sep 13;10(1):4180. doi: 10.1038/s41467-019-12121-9.

Structure of the thermo-sensitive TRP channel TRP1 from the alga Chlamydomonas reinhardtii.

Author information

1
Department of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168th Street, New York, NY, 10032, USA.
2
Integrated Program in Cellular, Molecular and Biomedical Studies, Columbia University, 650 West 168th Street, New York, NY, 10032, USA.
3
Department of Cancer Biology & Pharmacology, The University of Illinois College of Medicine at Peoria, One Illini Drive, Peoria, IL, 61605, USA.
4
Department of Cancer Biology & Pharmacology, The University of Illinois College of Medicine at Peoria, One Illini Drive, Peoria, IL, 61605, USA. zakharel@uic.edu.
5
Department of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168th Street, New York, NY, 10032, USA. as4005@cumc.columbia.edu.

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 PIP2. 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.

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