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Yorodumi- EMDB-13607: Structure of CtAtm1 in the occluded conformation with ATP bound -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-13607 | ||||||||||||
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Title | Structure of CtAtm1 in the occluded conformation with ATP bound | ||||||||||||
Map data | |||||||||||||
Sample |
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Keywords | ABC exporter / MEMBRANE PROTEIN | ||||||||||||
Function / homology | Function and homology information ABC-type transporter activity / mitochondrial inner membrane / ATP hydrolysis activity / ATP binding Similarity search - Function | ||||||||||||
Biological species | Chaetomium thermophilum var. thermophilum DSM 1495 (fungus) / Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus) | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.81 Å | ||||||||||||
Authors | Li P / Wang KT | ||||||||||||
Funding support | Denmark, 3 items
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Citation | Journal: Nat Commun / Year: 2022 Title: Structures of Atm1 provide insight into [2Fe-2S] cluster export from mitochondria. Authors: Ping Li / Amber L Hendricks / Yong Wang / Rhiza Lyne E Villones / Karin Lindkvist-Petersson / Gabriele Meloni / J A Cowan / Kaituo Wang / Pontus Gourdon / Abstract: In eukaryotes, iron-sulfur clusters are essential cofactors for numerous physiological processes, but these clusters are primarily biosynthesized in mitochondria. Previous studies suggest ...In eukaryotes, iron-sulfur clusters are essential cofactors for numerous physiological processes, but these clusters are primarily biosynthesized in mitochondria. Previous studies suggest mitochondrial ABCB7-type exporters are involved in maturation of cytosolic iron-sulfur proteins. However, the molecular mechanism for how the ABCB7-type exporters participate in this process remains elusive. Here, we report a series of cryo-electron microscopy structures of a eukaryotic homolog of human ABCB7, CtAtm1, determined at average resolutions ranging from 2.8 to 3.2 Å, complemented by functional characterization and molecular docking in silico. We propose that CtAtm1 accepts delivery from glutathione-complexed iron-sulfur clusters. A partially occluded state links cargo-binding to residues at the mitochondrial matrix interface that line a positively charged cavity, while the binding region becomes internalized and is partially divided in an early occluded state. Collectively, our findings substantially increase the understanding of the transport mechanism of eukaryotic ABCB7-type proteins. | ||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_13607.map.gz | 64.4 MB | EMDB map data format | |
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Header (meta data) | emd-13607-v30.xml emd-13607.xml | 15.4 KB 15.4 KB | Display Display | EMDB header |
Images | emd_13607.png | 25.4 KB | ||
Filedesc metadata | emd-13607.cif.gz | 5.9 KB | ||
Others | emd_13607_half_map_1.map.gz emd_13607_half_map_2.map.gz | 115.9 MB 115.9 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-13607 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-13607 | HTTPS FTP |
-Validation report
Summary document | emd_13607_validation.pdf.gz | 841.9 KB | Display | EMDB validaton report |
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Full document | emd_13607_full_validation.pdf.gz | 841.5 KB | Display | |
Data in XML | emd_13607_validation.xml.gz | 14 KB | Display | |
Data in CIF | emd_13607_validation.cif.gz | 16.3 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-13607 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-13607 | HTTPS FTP |
-Related structure data
Related structure data | 7pr1MC 7pqxC 7proC 7pruC 7psdC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_13607.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.832 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_13607_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_13607_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : atm1
Entire | Name: atm1 |
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Components |
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-Supramolecule #1: atm1
Supramolecule | Name: atm1 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: Chaetomium thermophilum var. thermophilum DSM 1495 (fungus) |
-Macromolecule #1: Putative iron-sulfur protein
Macromolecule | Name: Putative iron-sulfur protein / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus) Strain: DSM 1495 / CBS 144.50 / IMI 039719 |
Molecular weight | Theoretical: 77.199812 KDa |
Recombinant expression | Organism: Saccharomyces cerevisiae (brewer's yeast) |
Sequence | String: MSPRSRLLAS SLRGGLLLRP CSARRSTLLN PSPSPLRKAI FHTTSLRAFK NLAEIATSSK EDASSLKPKG KPSPPGDPLA TIEKTAAEQ RRADWAIIKQ MSRYLWPKDS WSDKARVLLA LSLLVGGKVL NVHVPFYFRE IIDRLNIDVA AVGGTVSAVA G AVIFAYGA ...String: MSPRSRLLAS SLRGGLLLRP CSARRSTLLN PSPSPLRKAI FHTTSLRAFK NLAEIATSSK EDASSLKPKG KPSPPGDPLA TIEKTAAEQ RRADWAIIKQ MSRYLWPKDS WSDKARVLLA LSLLVGGKVL NVHVPFYFRE IIDRLNIDVA AVGGTVSAVA G AVIFAYGA SRIGAVVSQE LRNAVFSSVA QKAIRRVATQ TFGHLLNLDL SFHLSKQTGG LTRAIDRGTK GISYLLTSMV FH IVPTALE IGMVCGILTY QFGWEFAAIT AATMAAYTAF TITTTAWRTK FRRQANAADN AASTVAVDSL INYEAVKYFN NEA YEIARY DKALQAYERS SIKVATSLAF LNSGQNIIFS SALTLMMWLG ARGVLAGDLS VGDLVLINQL VFQLSVPLNF LGSV YRELR QSLLDMETLF DLQKVNVTIR EAPNAKPLAL PKGGEIRFEN VTFGYYPDRP ILRNLSLTIP AGKKVAVVGP SGCGK STLL RLLFRSYDPQ QGKIFIDDQD IKSVTLESLR KSIGVVPQDT PLFNDTVELN IRYGNVNATQ EQVIAAAQKA HIHEKI ISW PHGYQTRVGE RGLMISGGEK QRLAVSRLIL KDPPLLFFDQ ATSALDTHTE QALMANINEV VKEKKRTALF VAHRLRT IY DADLIIVLKE GVVVEQGSHR ELMERDGVYA ELWMAQEMLH QGEAAEEPAE GEKAEEKK UniProtKB: Iron-sulfur clusters transporter ATM1, mitochondrial |
-Macromolecule #2: ADENOSINE-5'-TRIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 2 / Number of copies: 2 / Formula: ATP |
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Molecular weight | Theoretical: 507.181 Da |
Chemical component information | ChemComp-ATP: |
-Macromolecule #3: MAGNESIUM ION
Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 3 / Number of copies: 2 / Formula: MG |
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Molecular weight | Theoretical: 24.305 Da |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / Average electron dose: 40.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: PDB ENTRY |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 2.81 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 117631 |
Initial angle assignment | Type: RANDOM ASSIGNMENT |
Final angle assignment | Type: RANDOM ASSIGNMENT |