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	Mechanical activation opens a lipid-lined pore in OSCA ion channels.
Journal, issue, pages	Nature, Year 2024
Publish date	Apr 3, 2024
Authors	Yaoyao Han / Zijing Zhou / Ruitao Jin / Fei Dai / Yifan Ge / Xisan Ju / Xiaonuo Ma / Sitong He / Ling Yuan / Yingying Wang / Wei Yang / Xiaomin Yue / Zhongwen Chen / Yadong Sun / Ben Corry / Charles D Cox / Yixiao Zhang /
PubMed Abstract	OSCA/TMEM63 channels are the largest known family of mechanosensitive channels, playing critical roles in plant and mammalian mechanotransduction. Here we determined 44 cryogenic electron microscopy ...OSCA/TMEM63 channels are the largest known family of mechanosensitive channels, playing critical roles in plant and mammalian mechanotransduction. Here we determined 44 cryogenic electron microscopy structures of OSCA/TMEM63 channels in different environments to investigate the molecular basis of OSCA/TMEM63 channel mechanosensitivity. In nanodiscs, we mimicked increased membrane tension and observed a dilated pore with membrane access in one of the OSCA1.2 subunits. In liposomes, we captured the fully open structure of OSCA1.2 in the inside-in orientation, in which the pore shows a large lateral opening to the membrane. Unusually for ion channels, structural, functional and computational evidence supports the existence of a 'proteo-lipidic pore' in which lipids act as a wall of the ion permeation pathway. In the less tension-sensitive homologue OSCA3.1, we identified an 'interlocking' lipid tightly bound in the central cleft, keeping the channel closed. Mutation of the lipid-coordinating residues induced OSCA3.1 activation, revealing a conserved open conformation of OSCA channels. Our structures provide a global picture of the OSCA channel gating cycle, uncover the importance of bound lipids and show that each subunit can open independently. This expands both our understanding of channel-mediated mechanotransduction and channel pore formation, with important mechanistic implications for the TMEM16 and TMC protein families.
External links	Nature / PubMed:38570680
Methods	EM (single particle)
Resolution	3.11 - 4.49 Å
Structure data	38200 8xaj EMDB-38200, PDB-8xaj: Cryo-EM structure of OSCA1.2-liposome-inside-in open state Method: EM (single particle) / Resolution: 3.29 Å 38503 8xng EMDB-38503, PDB-8xng: Cryo-EM structure of OSCA1.2-liposome-inside-out closed state Method: EM (single particle) / Resolution: 3.56 Å 38611 8xry EMDB-38611, PDB-8xry: Cryo-EM structure of OSCA3.1-1.1ver(Y367N-G454S-Y458I)-open/open state Method: EM (single particle) / Resolution: 3.84 Å 38612 8xs0 EMDB-38612, PDB-8xs0: Cryo-EM structure of OSCA3.1-1.1ver(Y367N-G454S-Y458I)-open/'desensitized' state Method: EM (single particle) / Resolution: 3.89 Å 38614 8xs4 EMDB-38614, PDB-8xs4: Cryo-EM structure of OSCA1.2-DOPC-1:20-contracted1 state Method: EM (single particle) / Resolution: 3.23 Å 38615 8xs5 EMDB-38615, PDB-8xs5: Cryo-EM structure of OSCA1.2-DOPC-1:20-contracted2 state Method: EM (single particle) / Resolution: 3.33 Å 38721 8xvx EMDB-38721, PDB-8xvx: Cryo-EM structure of OSCA1.2-DOPC-1:20-expanded state Method: EM (single particle) / Resolution: 3.32 Å 38723 8xvy EMDB-38723, PDB-8xvy: Cryo-EM structure of OSCA3.1-2E(R611E-R619E)-closed/open state Method: EM (single particle) / Resolution: 3.71 Å 38724 8xvz EMDB-38724, PDB-8xvz: Cryo-EM structure of OSCA3.1-2E(R611E-R619E)-closed/'desensitized' state Method: EM (single particle) / Resolution: 3.78 Å 38725 8xw0 EMDB-38725, PDB-8xw0: Cryo-EM structure of OSCA3.1-GDN state Method: EM (single particle) / Resolution: 3.11 Å 38727 8xw1 EMDB-38727, PDB-8xw1: Cryo-EM structure of OSCA1.2-V335W-DDM state Method: EM (single particle) / Resolution: 4.49 Å 38728 8xw2 EMDB-38728, PDB-8xw2: Cryo-EM structure of OSCA1.2-DOPC-1:50-contracted state Method: EM (single particle) / Resolution: 3.59 Å 38729 8xw3 EMDB-38729, PDB-8xw3: Cryo-EM structure of OSCA1.2-DOPC-1:50-expanded state Method: EM (single particle) / Resolution: 3.63 Å 38730 8xw4 EMDB-38730, PDB-8xw4: Cryo-EM structure of TMEM63B-Digitonin state Method: EM (single particle) / Resolution: 3.84 Å
Chemicals	ChemComp-PCW: 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / DOPC, phospholipidYM ChemComp-P5S*: O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine / Phosphatidylserine
Source	arabidopsis thaliana (thale cress) homo sapiens (human)
Keywords	PLANT PROTEIN / OSCA/TMEM63 channel / mechanosensitive channel