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- EMDB-1593: Electron crystallographic reconstruction of human copper transpor... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-1593 | |||||||||
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Title | Electron crystallographic reconstruction of human copper transporter (hCTR1). | |||||||||
![]() | Volume map of human copper transporter (hCTR1) metal free. | |||||||||
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![]() | Cryo-EM / electron crystallography / 2D-crystal / membrane protein / copper | |||||||||
Function / homology | ![]() silver ion transmembrane transporter activity / plasma membrane copper ion transport / Metal ion SLC transporters / silver ion transmembrane transport / copper ion transmembrane transporter activity / copper ion import / vascular endothelial growth factor receptor-2 signaling pathway / copper ion transport / xenobiotic transport / xenobiotic transmembrane transporter activity ...silver ion transmembrane transporter activity / plasma membrane copper ion transport / Metal ion SLC transporters / silver ion transmembrane transport / copper ion transmembrane transporter activity / copper ion import / vascular endothelial growth factor receptor-2 signaling pathway / copper ion transport / xenobiotic transport / xenobiotic transmembrane transporter activity / intercalated disc / intracellular copper ion homeostasis / establishment of localization in cell / recycling endosome membrane / protein complex oligomerization / late endosome membrane / early endosome membrane / basolateral plasma membrane / angiogenesis / apical plasma membrane / copper ion binding / identical protein binding / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | electron crystallography / cryo EM / negative staining / Resolution: 7.0 Å | |||||||||
![]() | DeFeo CJ / Aller SG / Siluvai GS / Blackburn NJ / Unger VM | |||||||||
![]() | ![]() Title: Three-dimensional structure of the human copper transporter hCTR1. Authors: Christopher J De Feo / Stephen G Aller / Gnana S Siluvai / Ninian J Blackburn / Vinzenz M Unger / ![]() Abstract: Copper uptake proteins (CTRs), mediate cellular acquisition of the essential metal copper in all eukaryotes. Here, we report the structure of the human CTR1 protein solved by electron crystallography ...Copper uptake proteins (CTRs), mediate cellular acquisition of the essential metal copper in all eukaryotes. Here, we report the structure of the human CTR1 protein solved by electron crystallography to an in plane resolution of 7 A. Reminiscent of the design of traditional ion channels, trimeric hCTR1 creates a pore that stretches across the membrane bilayer at the interface between the subunits. Assignment of the helices identifies the second transmembrane helix as the key element lining the pore, and reveals how functionally important residues on this helix could participate in Cu(I)-coordination during transport. Aligned with and sealing both ends of the pore, extracellular and intracellular domains of hCTR1 appear to provide additional metal binding sites. Consistent with the existence of distinct metal binding sites, we demonstrate that hCTR1 stably binds 2 Cu(I)-ions through 3-coordinate Cu-S bonds, and that mutations in one of these putative binding sites results in a change of coordination chemistry. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 14.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 11.1 KB 11.1 KB | Display Display | ![]() |
Images | ![]() | 36.3 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 203.3 KB | Display | ![]() |
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Full document | ![]() | 202.5 KB | Display | |
Data in XML | ![]() | 5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | Volume map of human copper transporter (hCTR1) metal free. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. generated in cubic-lattice coordinate | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X: 1.01136 Å / Y: 1.01136 Å / Z: 1 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 177 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : human copper transporter hCTR1
Entire | Name: human copper transporter hCTR1 |
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Components |
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-Supramolecule #1000: human copper transporter hCTR1
Supramolecule | Name: human copper transporter hCTR1 / type: sample / ID: 1000 / Oligomeric state: trimer / Number unique components: 1 |
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Molecular weight | Theoretical: 66 KDa |
-Macromolecule #1: hCTR1
Macromolecule | Name: hCTR1 / type: protein_or_peptide / ID: 1 / Name.synonym: copper transporter / Number of copies: 3 / Oligomeric state: trimer / Recombinant expression: Yes |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 66 KDa |
Recombinant expression | Organism: ![]() |
Sequence | UniProtKB: High affinity copper uptake protein 1 |
-Experimental details
-Structure determination
Method | negative staining, cryo EM |
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![]() | electron crystallography |
Aggregation state | 2D array |
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Sample preparation
Concentration | 0.37 mg/mL |
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Buffer | pH: 7.4 / Details: 10mM MOPS, 280mM NaCl, 2.0 mM EDTA |
Staining | Type: NEGATIVE / Details: none |
Grid | Details: 300 mesh molybdenum grids |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 93 K / Instrument: HOMEMADE PLUNGER Details: Vitrification instrument: Home built plunger. no special treatment Method: Blot for 5 seconds before plunging |
Details | grown by dialysis |
Crystal formation | Details: grown by dialysis |
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Electron microscopy
Microscope | FEI TECNAI F20 |
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Temperature | Min: 93 K / Max: 93 K / Average: 93 K |
Alignment procedure | Legacy - Astigmatism: 230,000 times magnification |
Image recording | Category: FILM / Film or detector model: KODAK SO-163 FILM / Digitization - Scanner: ZEISS SCAI / Digitization - Sampling interval: 7.0 µm / Number real images: 58 / Average electron dose: 10 e/Å2 / Bits/pixel: 8 |
Electron beam | Acceleration voltage: 200 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2 mm / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.4 µm / Nominal magnification: 50000 |
Sample stage | Specimen holder: Gatan Side Entry / Specimen holder model: GATAN LIQUID NITROGEN / Tilt angle min: 1.2 / Tilt angle max: 46.2 / Tilt series - Axis1 - Min angle: 1.2 ° / Tilt series - Axis1 - Max angle: 46.2 ° |
Experimental equipment | ![]() Model: Tecnai F20 / Image courtesy: FEI Company |
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Image processing
Final reconstruction | Algorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 7.0 Å / Resolution method: OTHER / Software - Name: MRC |
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Crystal parameters | Unit cell - A: 89 Å / Unit cell - B: 89 Å / Unit cell - C: 400 Å / Unit cell - γ: 120 ° / Unit cell - α: 90 ° / Unit cell - β: 90 ° / Plane group: P 6 2 2 |
CTF correction | Details: Each image |