{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Shen X"],"funding":["Fudan University","China Postdoctoral Science Foundation","Ministry of Science and Technology of the People's Republic of China (Chinese Ministry of Science and Technology)","National Natural Science Foundation of China (National Science Foundation of China)"],"pagination":["8581"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12480533"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(1)"],"pubmed_abstract":["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 t"],"journal":["Nature communications"],"pubmed_title":["Molecular mechanisms of SLC30A10-mediated manganese transport."],"pmcid":["PMC12480533"],"funding_grant_id":["32171216","STI2030-Major Projects 2022ZD0212600","2023M730689","23216"],"pubmed_authors":["Zhang JK","Yang H","Sun P","Wang S","Guo X","Zhong H","Shen X","He R"],"additional_accession":[]},"is_claimable":false,"name":"Molecular mechanisms of SLC30A10-mediated manganese transport.","description":"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 t","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Sep","modification":"2026-06-04T00:00:45.274Z","creation":"2026-05-03T03:12:08.394Z"},"accession":"S-EPMC12480533","cross_references":{"pubmed":["41022720"],"doi":["10.1038/s41467-025-63616-7"]}}