8TDL

Cryo-EM structure of the wild-type AtMSL10 in saposin

Summary for 8TDL

• Entry DOI: 10.2210/pdb8tdl/pdb
• EMDB information: 41164 41165 41166 41168
• Descriptor: Mechanosensitive ion channel protein 10 (1 entity in total)
• Functional Keywords: ion channels, mechanosensitive channels, heptamer, arabidopsis thaliana, transport protein
• Biological source: Arabidopsis thaliana (thale cress)
• Total number of polymer chains: 7
• Total formula weight: 587688.93

Authors

Zhang, J.,Yuan, P. (deposition date: 2023-07-03, release date: 2023-10-18)

Primary citation

Zhang, J.,Maksaev, G.,Yuan, P.
Open structure and gating of the Arabidopsis mechanosensitive ion channel MSL10.
Nat Commun, 14:6284-6284, 2023

PubMed Abstract: Plants are challenged by drastically different osmotic environments during growth and development. Adaptation to these environments often involves mechanosensitive ion channels that can detect and respond to mechanical force. In the model plant Arabidopsis thaliana, the mechanosensitive channel MSL10 plays a crucial role in hypo-osmotic shock adaptation and programmed cell death induction, but the molecular basis of channel function remains poorly understood. Here, we report a structural and electrophysiological analysis of MSL10. The cryo-electron microscopy structures reveal a distinct heptameric channel assembly. Structures of the wild-type channel in detergent and lipid environments, and in the absence of membrane tension, capture an open conformation. Furthermore, structural analysis of a non-conductive mutant channel demonstrates that reorientation of phenylalanine side chains alone, without main chain rearrangements, may generate the hydrophobic gate. Together, these results reveal a distinct gating mechanism and advance our understanding of mechanotransduction.

PubMed: 37805510
DOI: 10.1038/s41467-023-42117-5

Experimental method

ELECTRON MICROSCOPY (3.6 Å)