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Yorodumi- PDB-9kvz: Cryo-EM structure of SLC30A10 in the absence of Mn2+, determined ... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9kvz | |||||||||
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| Title | Cryo-EM structure of SLC30A10 in the absence of Mn2+, determined in inward-facing conformation | |||||||||
Components | Calcium/manganese antiporter SLC30A10 | |||||||||
Keywords | TRANSPORT PROTEIN / Manganese Transpoter / SLC30A10 / ZnT10 | |||||||||
| Function / homology | Function and homology informationmanganese ion export across plasma membrane / calcium:manganese antiporter activity / detoxification of zinc ion / zinc ion import into organelle / Metal ion SLC transporters / manganese ion transport / intracellular manganese ion homeostasis / manganese ion transmembrane transporter activity / zinc ion transmembrane transporter activity / zinc ion transmembrane transport ...manganese ion export across plasma membrane / calcium:manganese antiporter activity / detoxification of zinc ion / zinc ion import into organelle / Metal ion SLC transporters / manganese ion transport / intracellular manganese ion homeostasis / manganese ion transmembrane transporter activity / zinc ion transmembrane transporter activity / zinc ion transmembrane transport / intracellular zinc ion homeostasis / cellular response to angiotensin / recycling endosome / epidermal growth factor receptor signaling pathway / recycling endosome membrane / early endosome membrane / early endosome / positive regulation of ERK1 and ERK2 cascade / Golgi membrane / Golgi apparatus / membrane / plasma membrane Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.94 Å | |||||||||
Authors | Yang, H. / Zhang, J.K. / Shen, X. | |||||||||
| Funding support | China, 2items
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Citation | Journal: Nat Commun / Year: 2025Title: Molecular mechanisms of SLC30A10-mediated manganese transport. Authors: Xurui Shen / Jinlun Kylian Zhang / Peixin Sun / Huiwen Zhong / Rui He / Shiliang Wang / Xiaojun Guo / Hanting Yang / ![]() 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 ...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. | |||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9kvz.cif.gz | 123.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9kvz.ent.gz | 92.4 KB | Display | PDB format |
| PDBx/mmJSON format | 9kvz.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9kvz_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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| Full document | 9kvz_full_validation.pdf.gz | 1.2 MB | Display | |
| Data in XML | 9kvz_validation.xml.gz | 31.8 KB | Display | |
| Data in CIF | 9kvz_validation.cif.gz | 45.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kv/9kvz ftp://data.pdbj.org/pub/pdb/validation_reports/kv/9kvz | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 62605MC ![]() 9kvxC ![]() 9kvyC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 52740.832 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SLC30A10, ZNT10, ZNT8 / Production host: Homo sapiens (human) / References: UniProt: Q6XR72Has protein modification | Y | |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: SLC30A10 dimer of inward-facing at APO state / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.4 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1800 nm / Nominal defocus min: 800 nm |
| Image recording | Electron dose: 51.22 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
| EM software | Name: PHENIX / Version: 1.20.1_4487 / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.94 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 225307 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 2.94 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi



Homo sapiens (human)
China, 2items
Citation




PDBj

FIELD EMISSION GUN