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-Structure paper
| タイトル | Structure of mechanically activated ion channel OSCA2.3 reveals mobile elements in the transmembrane domain. |
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| ジャーナル・号・ページ | Structure, Vol. 32, Issue 2, Page 157-167.e5, Year 2024 |
| 掲載日 | 2024年2月1日 |
著者 | Sebastian Jojoa-Cruz / Batuujin Burendei / Wen-Hsin Lee / Andrew B Ward / ![]() |
| PubMed 要旨 | Members of the OSCA/TMEM63 family are mechanically activated ion channels and structures of some OSCA members have revealed the architecture of these channels and structural features that are ...Members of the OSCA/TMEM63 family are mechanically activated ion channels and structures of some OSCA members have revealed the architecture of these channels and structural features that are potentially involved in mechanosensation. However, these structures are all in a similar state and information about the motion of different elements of the structure is limited, preventing a deeper understanding of how these channels work. Here, we used cryoelectron microscopy to determine high-resolution structures of Arabidopsis thaliana OSCA1.2 and OSCA2.3 in peptidiscs. The structure of OSCA1.2 matches previous structures of the same protein in different environments. Yet, in OSCA2.3, the TM6a-TM7 linker adopts a different conformation that constricts the pore on its cytoplasmic side. Furthermore, coevolutionary sequence analysis uncovered a conserved interaction between the TM6a-TM7 linker and the beam-like domain (BLD). Our results reveal conformational heterogeneity and differences in conserved interactions between the TMD and BLD among members of the OSCA family. |
リンク | Structure / PubMed:38103547 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 2.7 - 2.8 Å |
| 構造データ | EMDB-41043, PDB-8t56: EMDB-41044, PDB-8t57: |
| 化合物 | ![]() ChemComp-Y01: ![]() ChemComp-PLM: ![]() ChemComp-LBN: ![]() ChemComp-CLR: |
| 由来 |
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キーワード | MEMBRANE PROTEIN / mechanically activated ion channel |
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