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Yorodumi- EMDB-24183: Structure of AtAtm3 in the inward-facing conformation with GSSG bound -
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Open data
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Basic information
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| Title | Structure of AtAtm3 in the inward-facing conformation with GSSG bound | |||||||||
Map data | AtAtm3 in the inward-facing conformation with GSSG bound | |||||||||
Sample |
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Keywords | ATPase / MEMBRANE PROTEIN | |||||||||
| Function / homology | Function and homology informationregulation of chlorophyll biosynthetic process / regulation of catalytic activity / chloroplast organization / root development / pollen development / Mo-molybdopterin cofactor biosynthetic process / chloroplast envelope / plastid / chromosome organization / response to cadmium ion ...regulation of chlorophyll biosynthetic process / regulation of catalytic activity / chloroplast organization / root development / pollen development / Mo-molybdopterin cofactor biosynthetic process / chloroplast envelope / plastid / chromosome organization / response to cadmium ion / ABC-type transporter activity / chloroplast / iron ion transport / response to lead ion / intracellular iron ion homeostasis / mitochondrial inner membrane / ATP hydrolysis activity / mitochondrion / ATP binding Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.6 Å | |||||||||
Authors | Fan C / Rees DC | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: Elife / Year: 2022Title: Glutathione binding to the plant Atm3 transporter and implications for the conformational coupling of ABC transporters. Authors: Chengcheng Fan / Douglas C Rees / ![]() Abstract: The ATP binding cassette (ABC) transporter of mitochondria (Atm) from (Atm3) has been implicated in the maturation of cytosolic iron-sulfur proteins and heavy metal detoxification, plausibly by ...The ATP binding cassette (ABC) transporter of mitochondria (Atm) from (Atm3) has been implicated in the maturation of cytosolic iron-sulfur proteins and heavy metal detoxification, plausibly by exporting glutathione derivatives. Using single-particle cryo-electron microscopy, we have determined four structures of Atm3 in three different conformational states: two inward-facing conformations (with and without bound oxidized glutathione [GSSG]), together with closed and outward-facing states stabilized by MgADP-VO. These structures not only provide a structural framework for defining the alternating access transport cycle, but also reveal the paucity of cysteine residues in the glutathione binding site that could potentially form inhibitory mixed disulfides with GSSG. Despite extensive efforts, we were unable to prepare the ternary complex of Atm3 containing both GSSG and MgATP. A survey of structurally characterized type IV ABC transporters that includes Atm3 establishes that while nucleotides are found associated with all conformational states, they are effectively required to stabilize occluded, closed, and outward-facing conformations. In contrast, transport substrates have only been observed associated with inward-facing conformations. The absence of structures with dimerized nucleotide binding domains containing both nucleotide and transport substrate suggests that this form of the ternary complex exists only transiently during the transport cycle. | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_24183.map.gz | 97 MB | EMDB map data format | |
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| Header (meta data) | emd-24183-v30.xml emd-24183.xml | 17.3 KB 17.3 KB | Display Display | EMDB header |
| Images | emd_24183.png | 88.4 KB | ||
| Filedesc metadata | emd-24183.cif.gz | 6.2 KB | ||
| Others | emd_24183_half_map_1.map.gz emd_24183_half_map_2.map.gz | 95.3 MB 95.3 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-24183 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-24183 | HTTPS FTP |
-Validation report
| Summary document | emd_24183_validation.pdf.gz | 1.1 MB | Display | EMDB validaton report |
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| Full document | emd_24183_full_validation.pdf.gz | 1.1 MB | Display | |
| Data in XML | emd_24183_validation.xml.gz | 13.4 KB | Display | |
| Data in CIF | emd_24183_validation.cif.gz | 15.7 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-24183 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-24183 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 7n59MC ![]() 7n58C ![]() 7n5aC ![]() 7n5bC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_24183.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | AtAtm3 in the inward-facing conformation with GSSG bound | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.855 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: AtAtm3 in the inward-facing conformation with GSSG bound
| File | emd_24183_half_map_1.map | ||||||||||||
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| Annotation | AtAtm3 in the inward-facing conformation with GSSG bound | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: AtAtm3 in the inward-facing conformation with GSSG bound
| File | emd_24183_half_map_2.map | ||||||||||||
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| Annotation | AtAtm3 in the inward-facing conformation with GSSG bound | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : AtAtm3 in detergent
| Entire | Name: AtAtm3 in detergent |
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| Components |
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-Supramolecule #1: AtAtm3 in detergent
| Supramolecule | Name: AtAtm3 in detergent / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 140 KDa |
-Macromolecule #1: ABC transporter B family member 25, mitochondrial
| Macromolecule | Name: ABC transporter B family member 25, mitochondrial / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 81.793344 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MSRGSRFVRA PGLLLCRVNL QPQPKIPSFS YSLRSDYRLH NGFSNYIRRN SIRTSPVINA FLSDNSPSPS PSPSPIRFVQ RSSMLNGRL FSTSTPNPDQ TTTKTKEIKT TSSDSDSAMA DMKILRTLAG YLWMRDNPEF RFRVIAALGF LVGAKVLNVQ V PFLFKLAV ...String: MSRGSRFVRA PGLLLCRVNL QPQPKIPSFS YSLRSDYRLH NGFSNYIRRN SIRTSPVINA FLSDNSPSPS PSPSPIRFVQ RSSMLNGRL FSTSTPNPDQ TTTKTKEIKT TSSDSDSAMA DMKILRTLAG YLWMRDNPEF RFRVIAALGF LVGAKVLNVQ V PFLFKLAV DWLASATGTG ASLTTFAATN PTLLTVFATP AAVLIGYGIA RTGSSAFNEL RTAVFSKVAL RTIRSVSRKV FS HLHDLDL RYHLSRETGG LNRIIDRGSR AINFILSAMV FNVVPTILEI SMVSGILAYK FGAAFAWITS LSVGSYIVFT LAV TQWRTK FRKAMNKADN DASTRAIDSL INYETVKYFN NEGYEAEKYD QFLKKYEDAA LQTQRSLAFL NFGQSIIFST ALST AMVLC SQGIMNGQMT VGDLVMVNGL LFQLSLPLNF LGSVYRETIQ SLVDMKSMFQ LLEEKSDITN TSDAKPLVLK GGNIE FENV HFSYLPERKI LDGISFVVPA GKSVAIVGTS GSGKSTILRM LFRFFDTDSG NIRIDGQDIK EVRLDSLRSS IGVVPQ DTV LFNDTIFHNI HYGRLSATEE EVYEAARRAA IHETISNFPD KYSTIVGERG LKLSGGEKQR VALARTFLKS PAILLCD EA TSALDSTTEA EILNALKALA SNRTSIFIAH RLTTAMQCDE IVVLENGKVV EQGPHDELLG KSGRYAQLWT QQNSSVDM L DAAIKLEAAA LEHHHHHH UniProtKB: ABC transporter B family member 25, mitochondrial |
-Macromolecule #2: OXIDIZED GLUTATHIONE DISULFIDE
| Macromolecule | Name: OXIDIZED GLUTATHIONE DISULFIDE / type: ligand / ID: 2 / Number of copies: 1 / Formula: GDS |
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| Molecular weight | Theoretical: 612.631 Da |
| Chemical component information | ![]() ChemComp-GDS: |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 1 mg/mL | |||||||||
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| Buffer | pH: 7.5 Component:
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| Grid | Model: UltrAuFoil R1.2/1.3 / Support film - Material: GOLD / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE | |||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 295 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number real images: 6426 / Average exposure time: 2.7 sec. / Average electron dose: 60.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 105000 |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords
Authors
United States, 1 items
Citation








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Processing
FIELD EMISSION GUN

