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TitleMolecular mechanisms of SLC30A10-mediated manganese transport.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 8581, Year 2025
Publish dateSep 29, 2025
AuthorsXurui Shen / Jinlun Kylian Zhang / Peixin Sun / Huiwen Zhong / Rui He / Shiliang Wang / Xiaojun Guo / Hanting Yang /
PubMed AbstractManganese 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.
External linksNat Commun / PubMed:41022720 / PubMed Central
MethodsEM (single particle)
Resolution2.79 - 3.34 Å
Structure data

62603

9kvx

EMDB-62603, PDB-9kvx:
Cryo-EM structure of SLC30A10 in Mn2+-bound state, determined in inward-facing conformation
Method: EM (single particle) / Resolution: 2.79 Å

62604

9kvy

EMDB-62604, PDB-9kvy:
Cryo-EM structure of SLC30A10, determined in asymmetric conformations-one subunit in an inward-facing Mn2+-bound and the other in an outward-facing Mn2+-unbound conformation
Method: EM (single particle) / Resolution: 3.34 Å

62605

9kvz

EMDB-62605, PDB-9kvz:
Cryo-EM structure of SLC30A10 in the absence of Mn2+, determined in inward-facing conformation
Method: EM (single particle) / Resolution: 2.94 Å

Chemicals

ChemComp-MN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / Manganese Transpoter / SLC30A10 / ZnT10

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