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-Structure paper
| タイトル | Molecular mechanisms of SLC30A10-mediated manganese transport. |
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| ジャーナル・号・ページ | Nat Commun, Vol. 16, Issue 1, Page 8581, Year 2025 |
| 掲載日 | 2025年9月29日 |
著者 | Xurui Shen / Jinlun Kylian Zhang / Peixin Sun / Huiwen Zhong / Rui He / Shiliang Wang / Xiaojun Guo / Hanting Yang / ![]() |
| PubMed 要旨 | Manganese ion (Mn²⁺) is crucial for various physiological processes, yet excessive levels disrupt cellular homeostasis and impair the function of multiple organelles. The transporter SLC30A10 ...Manganese ion (Mn²⁺) is crucial for various physiological processes, yet excessive levels disrupt cellular homeostasis and impair the function of multiple organelles. The transporter SLC30A10 plays a pivotal role in Mn²⁺ homeostasis by exporting Mn²⁺ from cells, preventing toxic effects. Mutations in the SLC30A10 gene result in Mn²⁺ accumulation and lead to disorders such as hypermanganesemia with dystonia 1 (HMNDYT1). Despite its physiological significance, the structural basis underlying Mn²⁺ binding and the detailed transport mechanisms of SLC30A10 remain unknown. Here, we present diverse conformations of high-resolution cryo-electron microscopy (cryo-EM) structures that reveal a Mn²⁺-binding site in SLC30A10, setting it apart from other SLC30 family transporters. Furthermore, we show that the HMNDYT1-associated D40A mutation interrupts Mn²⁺ binding and transport, identifying D40 as a potential therapeutic target. These findings provide structural insights into Mn²⁺ transport mechanisms mediated by SLC30A10, advancing our understanding of Mn²⁺ binding and potential targets for future therapeutic exploration. |
リンク | Nat Commun / PubMed:41022720 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 2.79 - 3.34 Å |
| 構造データ | EMDB-62603, PDB-9kvx: EMDB-62604, PDB-9kvy: EMDB-62605, PDB-9kvz: |
| 化合物 | ![]() ChemComp-MN: ![]() ChemComp-HOH: |
| 由来 |
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キーワード | TRANSPORT PROTEIN / Manganese Transpoter / SLC30A10 / ZnT10 |
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