Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Open structure and gating of the Arabidopsis mechanosensitive ion channel MSL10.
Journal, issue, pages	Nat Commun, Vol. 14, Issue 1, Page 6284, Year 2023
Publish date	Oct 7, 2023
Authors	Jingying Zhang / Grigory Maksaev / Peng Yuan /
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 ...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.
External links	Nat Commun / PubMed:37805510 / PubMed Central
Methods	EM (single particle)
Resolution	3.5 - 3.7 Å
Structure data	41164 8tdj EMDB-41164, PDB-8tdj: Cryo-EM structure of the wild-type AtMSL10 in GDN Method: EM (single particle) / Resolution: 3.7 Å 41165 8tdk EMDB-41165, PDB-8tdk: Cryo-EM structure of AtMSL10-G556V Method: EM (single particle) / Resolution: 3.5 Å 41166 8tdl EMDB-41166, PDB-8tdl: Cryo-EM structure of the wild-type AtMSL10 in saposin Method: EM (single particle) / Resolution: 3.6 Å 41168 8tdm EMDB-41168, PDB-8tdm: Cryo-EM structure of AtMSL10-K539E Method: EM (single particle) / Resolution: 3.7 Å
Source	arabidopsis thaliana (thale cress)
Keywords	TRANSPORT PROTEIN / ion channels / mechanosensitive channels / heptamer / Arabidopsis thaliana