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Yorodumi- EMDB-14429: Structure of the Escherichia coli formate hydrogenlyase complex (... -
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-Basic information
Entry | Database: EMDB / ID: EMD-14429 | |||||||||
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Title | Structure of the Escherichia coli formate hydrogenlyase complex (anaerobic preparation, without formate dehydrogenase H) | |||||||||
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Function / homology | Function and homology information formate oxidation / formate dehydrogenase complex / plasma membrane respiratory chain complex I / anaerobic electron transport chain / glucose catabolic process / anaerobic respiration / oxidoreductase activity, acting on NAD(P)H / nickel cation binding / NADH dehydrogenase (ubiquinone) activity / quinone binding ...formate oxidation / formate dehydrogenase complex / plasma membrane respiratory chain complex I / anaerobic electron transport chain / glucose catabolic process / anaerobic respiration / oxidoreductase activity, acting on NAD(P)H / nickel cation binding / NADH dehydrogenase (ubiquinone) activity / quinone binding / ATP synthesis coupled electron transport / aerobic respiration / NAD binding / 4 iron, 4 sulfur cluster binding / membrane => GO:0016020 / oxidoreductase activity / membrane / metal ion binding / plasma membrane Similarity search - Function | |||||||||
Biological species | Escherichia coli (E. coli) / Escherichia coli K-12 (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.6 Å | |||||||||
Authors | Steinhilper R / Murphy BJ | |||||||||
Funding support | Germany, 1 items
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Citation | Journal: Nat Commun / Year: 2022 Title: Structure of the membrane-bound formate hydrogenlyase complex from Escherichia coli. Authors: Ralf Steinhilper / Gabriele Höff / Johann Heider / Bonnie J Murphy / Abstract: The prototypical hydrogen-producing enzyme, the membrane-bound formate hydrogenlyase (FHL) complex from Escherichia coli, links formate oxidation at a molybdopterin-containing formate dehydrogenase ...The prototypical hydrogen-producing enzyme, the membrane-bound formate hydrogenlyase (FHL) complex from Escherichia coli, links formate oxidation at a molybdopterin-containing formate dehydrogenase to proton reduction at a [NiFe] hydrogenase. It is of intense interest due to its ability to efficiently produce H during fermentation, its reversibility, allowing H-dependent CO reduction, and its evolutionary link to respiratory complex I. FHL has been studied for over a century, but its atomic structure remains unknown. Here we report cryo-EM structures of FHL in its aerobically and anaerobically isolated forms at resolutions reaching 2.6 Å. This includes well-resolved density for conserved loops linking the soluble and membrane arms believed to be essential in coupling enzymatic turnover to ion translocation across the membrane in the complex I superfamily. We evaluate possible structural determinants of the bias toward hydrogen production over its oxidation and describe an unpredicted metal-binding site near the interface of FdhF and HycF subunits that may play a role in redox-dependent regulation of FdhF interaction with the complex. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_14429.map.gz | 95.7 MB | EMDB map data format | |
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Header (meta data) | emd-14429-v30.xml emd-14429.xml | 23.9 KB 23.9 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_14429_fsc.xml | 10.7 KB | Display | FSC data file |
Images | emd_14429.png | 87.1 KB | ||
Masks | emd_14429_msk_1.map | 103 MB | Mask map | |
Others | emd_14429_half_map_1.map.gz emd_14429_half_map_2.map.gz | 95.5 MB 95.5 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-14429 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-14429 | HTTPS FTP |
-Related structure data
Related structure data | 7z0sMC 7z0tC 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_14429.map.gz / Format: CCP4 / Size: 103 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: 0.831 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | emd_14429_msk_1.map | ||||||||||||
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Density Histograms |
-Half map: #2
File | emd_14429_half_map_1.map | ||||||||||||
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Density Histograms |
-Half map: #1
File | emd_14429_half_map_2.map | ||||||||||||
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Density Histograms |
-Sample components
+Entire : Escherichia coli formate hydrogenlyase complex without formate de...
+Supramolecule #1: Escherichia coli formate hydrogenlyase complex without formate de...
+Macromolecule #1: Formate hydrogenlyase subunit 3
+Macromolecule #2: Formate hydrogenlyase subunit 5
+Macromolecule #3: Formate hydrogenlyase subunit 2
+Macromolecule #4: Formate hydrogenlyase subunit 7
+Macromolecule #5: Formate hydrogenlyase subunit 6
+Macromolecule #6: Formate hydrogenlyase subunit 4
+Macromolecule #7: CARDIOLIPIN
+Macromolecule #8: PHOSPHATIDYLETHANOLAMINE
+Macromolecule #9: NICKEL (II) ION
+Macromolecule #10: CARBONMONOXIDE-(DICYANO) IRON
+Macromolecule #11: 1-CIS-9-OCTADECANOYL-2-CIS-9-HEXADECANOYL PHOSPHATIDYL GLYCEROL
+Macromolecule #12: IRON/SULFUR CLUSTER
+Macromolecule #13: FE (III) ION
+Macromolecule #14: Lauryl Maltose Neopentyl Glycol
+Macromolecule #15: water
-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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Grid | Model: C-flat-1.2/1.3 / Material: COPPER / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 61.0 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |