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-Structure paper
タイトル | Structural basis for the activity regulation of Salt Overly Sensitive 1 in Arabidopsis salt tolerance. |
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ジャーナル・号・ページ | Nat Plants, Vol. 9, Issue 11, Page 1915-1923, Year 2023 |
掲載日 | 2023年10月26日 |
著者 | Yanming Zhang / Jiaqi Zhou / Xuping Ni / Qinrui Wang / Yutian Jia / Xia Xu / Haoyang Wu / Peng Fu / Han Wen / Yan Guo / Guanghui Yang / |
PubMed 要旨 | The plasma membrane Na/H exchanger Salt Overly Sensitive 1 (SOS1) is crucial for plant salt tolerance. Unlike typical sodium/proton exchangers, SOS1 contains a large cytoplasmic domain (CPD) that ...The plasma membrane Na/H exchanger Salt Overly Sensitive 1 (SOS1) is crucial for plant salt tolerance. Unlike typical sodium/proton exchangers, SOS1 contains a large cytoplasmic domain (CPD) that regulates Na/H exchange activity. However, the underlying modulation mechanism remains unclear. Here we report the structures of SOS1 from Arabidopsis thaliana in two conformations, primarily differing in CPD flexibility. The CPD comprises an interfacial domain, a cyclic nucleotide-binding domain-like domain (CNBD-like domain) and an autoinhibition domain. Through yeast cell-based Na tolerance test, we reveal the regulatory role of the interfacial domain and the activation role of the CNBD-like domain. The CPD forms a negatively charged cavity that is connected to the ion binding site. The transport of Na may be coupled with the conformational change of CPD. These findings provide structural and functional insight into SOS1 activity regulation. |
リンク | Nat Plants / PubMed:37884652 |
手法 | EM (単粒子) |
解像度 | 2.87 - 3.67 Å |
構造データ | EMDB-36076, PDB-8jda: EMDB-36077, PDB-8jd9: |
化合物 | ChemComp-PC1: |
由来 |
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キーワード | MEMBRANE PROTEIN / Sodium / Proton |