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Yorodumi- EMDB-55598: Structure of a stalled E. coli 70S RNC-NuoK-70 in complex with th... -
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Basic information
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| Title | Structure of a stalled E. coli 70S RNC-NuoK-70 in complex with the membrane protein insertase SecYEG-YidC | |||||||||
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Keywords | 70S Ribosome / SecYEG translocon / YidC / NuoK / PROTEIN TRANSPORT | |||||||||
| Function / homology | Function and homology informationmembrane insertase activity / cell envelope Sec protein transport complex / protein transport by the Sec complex / intracellular protein transmembrane transport / protein-transporting ATPase activity / NADH dehydrogenase (quinone) (non-electrogenic) activity / Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions / SRP-dependent cotranslational protein targeting to membrane, translocation / NADH dehydrogenase complex / signal sequence receptor activity ...membrane insertase activity / cell envelope Sec protein transport complex / protein transport by the Sec complex / intracellular protein transmembrane transport / protein-transporting ATPase activity / NADH dehydrogenase (quinone) (non-electrogenic) activity / Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions / SRP-dependent cotranslational protein targeting to membrane, translocation / NADH dehydrogenase complex / signal sequence receptor activity / negative regulation of cytoplasmic translational initiation / protein insertion into membrane / Secretion of toxins / transcription antitermination factor activity, RNA binding / ornithine decarboxylase inhibitor activity / transmembrane protein transporter activity / protein secretion / misfolded RNA binding / Group I intron splicing / RNA folding / quinone binding / ATP synthesis coupled electron transport / transcriptional attenuation / endoribonuclease inhibitor activity / positive regulation of ribosome biogenesis / RNA-binding transcription regulator activity / four-way junction DNA binding / negative regulation of cytoplasmic translation / DnaA-L2 complex / regulation of mRNA stability / translation repressor activity / negative regulation of translational initiation / negative regulation of DNA-templated DNA replication initiation / mRNA regulatory element binding translation repressor activity / positive regulation of RNA splicing / regulation of DNA-templated transcription elongation / transcription elongation factor complex / response to reactive oxygen species / cytosolic ribosome assembly / ribosome assembly / assembly of large subunit precursor of preribosome / transcription antitermination / DNA endonuclease activity / translational initiation / regulation of cell growth / DNA-templated transcription termination / intracellular protein transport / response to radiation / maintenance of translational fidelity / mRNA 5'-UTR binding / regulation of translation / large ribosomal subunit / transferase activity / ribosomal small subunit assembly / protein folding / ribosome binding / ribosome biogenesis / ribosomal small subunit biogenesis / 5S rRNA binding / protein-containing complex assembly / ribosomal large subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / response to antibiotic / negative regulation of DNA-templated transcription / hydrolase activity / mRNA binding / DNA binding / RNA binding / zinc ion binding / membrane / plasma membrane / cytoplasm / cytosol Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.85 Å | |||||||||
Authors | Rosales-Hernandez C / Busch M / Kamel M / Beckmann R / Kedrov A | |||||||||
| Funding support | Germany, 1 items
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Citation | Journal: EMBO J / Year: 2026Title: Substrate-induced assembly and functional mechanism of the membrane protein insertase SecYEG-YidC. Authors: Max Busch / Cristian Rosales-Hernandez / Michael Kamel / Yulia Schaumkessel / Eli O van der Sluis / Otto Berninghausen / Thomas Becker / Roland Beckmann / Alexej Kedrov / ![]() Abstract: The Sec translocon and the YidC/Oxa1-type insertases universally mediate biogenesis of α-helical membrane proteins, but the molecular basis of their cooperation has remained disputed. Recent ...The Sec translocon and the YidC/Oxa1-type insertases universally mediate biogenesis of α-helical membrane proteins, but the molecular basis of their cooperation has remained disputed. Recent discovery of multi-subunit insertases assembled at the back of the translocon in fungi and higher eukaryotes has raised questions about the architecture and mechanism of the putative bacterial ortholog SecYEG-YidC. Here, we combine cryogenic electron microscopy with cell-free protein synthesis to visualize biogenesis of the SecYEG/YidC-dependent multipass membrane protein NuoK. The nascent chain of NuoK does not enter the lateral gate of SecYEG but instead crosses the translocon towards its back side, where YidC is recruited in the nascent substrate-dependent manner. The SecY-YidC interface promotes folding of the transmembrane helices before insertion, consistent with thermodynamic principles of membrane protein folding. YidC forms extensive contacts with the nascent chain, suggesting its key role in the insertion event. These findings provide mechanistic insight into membrane protein insertases, support evolutionary conservation of a gate-independent insertion route, and expand current models of membrane protein biogenesis. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_55598.map.gz | 574.6 MB | EMDB map data format | |
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| Header (meta data) | emd-55598-v30.xml emd-55598.xml | 78.3 KB 78.3 KB | Display Display | EMDB header |
| Images | emd_55598.png | 44.4 KB | ||
| Filedesc metadata | emd-55598.cif.gz | 15.9 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-55598 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-55598 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9t5xMC ![]() 55568 ![]() 55570 ![]() 55571 ![]() 9rbfC C: citing same article ( M: atomic model generated by this map |
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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_55598.map.gz / Format: CCP4 / Size: 1.2 GB / 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: 0.727 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
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Sample components
+Entire : E. coli 70S RNC-NuoK-70 in complex with the membrane protein inse...
+Supramolecule #1: E. coli 70S RNC-NuoK-70 in complex with the membrane protein inse...
+Macromolecule #1: Large ribosomal subunit protein bL33
+Macromolecule #2: Large ribosomal subunit protein bL34
+Macromolecule #3: Large ribosomal subunit protein bL35
+Macromolecule #4: Large ribosomal subunit protein bL36A
+Macromolecule #5: Large ribosomal subunit protein bL31A
+Macromolecule #7: Protein translocase subunit SecY
+Macromolecule #8: Protein translocase subunit SecE
+Macromolecule #9: Protein-export membrane protein SecG
+Macromolecule #10: Membrane protein insertase YidC
+Macromolecule #12: Small ribosomal subunit protein uS2
+Macromolecule #13: Small ribosomal subunit protein uS3
+Macromolecule #14: Small ribosomal subunit protein uS4
+Macromolecule #15: Small ribosomal subunit protein uS5
+Macromolecule #16: Small ribosomal subunit protein bS6, fully modified isoform
+Macromolecule #17: Small ribosomal subunit protein uS7
+Macromolecule #18: Small ribosomal subunit protein uS8
+Macromolecule #19: Small ribosomal subunit protein uS9
+Macromolecule #20: Small ribosomal subunit protein uS10
+Macromolecule #21: Small ribosomal subunit protein uS11
+Macromolecule #22: Small ribosomal subunit protein uS12
+Macromolecule #23: Small ribosomal subunit protein uS13
+Macromolecule #24: Small ribosomal subunit protein uS14
+Macromolecule #25: Small ribosomal subunit protein uS15
+Macromolecule #26: Small ribosomal subunit protein bS16
+Macromolecule #27: Small ribosomal subunit protein uS17
+Macromolecule #28: Small ribosomal subunit protein bS18
+Macromolecule #29: Small ribosomal subunit protein uS19
+Macromolecule #30: Small ribosomal subunit protein bS20
+Macromolecule #31: Small ribosomal subunit protein bS21
+Macromolecule #32: NADH-quinone oxidoreductase subunit K
+Macromolecule #38: Large ribosomal subunit protein uL2
+Macromolecule #39: Large ribosomal subunit protein uL3
+Macromolecule #40: Large ribosomal subunit protein uL4
+Macromolecule #41: Large ribosomal subunit protein uL5
+Macromolecule #42: Large ribosomal subunit protein uL6
+Macromolecule #43: Large ribosomal subunit protein bL9
+Macromolecule #44: Large ribosomal subunit protein uL13
+Macromolecule #45: Large ribosomal subunit protein uL14
+Macromolecule #46: Large ribosomal subunit protein uL15
+Macromolecule #47: 50S ribosomal protein L16
+Macromolecule #48: Large ribosomal subunit protein bL17
+Macromolecule #49: Large ribosomal subunit protein uL18
+Macromolecule #50: Large ribosomal subunit protein bL19
+Macromolecule #51: Large ribosomal subunit protein bL20
+Macromolecule #52: Large ribosomal subunit protein bL21
+Macromolecule #53: Large ribosomal subunit protein uL22
+Macromolecule #54: Large ribosomal subunit protein uL23
+Macromolecule #55: Large ribosomal subunit protein uL24
+Macromolecule #56: Large ribosomal subunit protein bL25
+Macromolecule #57: Large ribosomal subunit protein bL27
+Macromolecule #58: Large ribosomal subunit protein bL28
+Macromolecule #59: Large ribosomal subunit protein uL29
+Macromolecule #60: Large ribosomal subunit protein uL30
+Macromolecule #61: Large ribosomal subunit protein bL32
+Macromolecule #6: E-site tRNA
+Macromolecule #11: 16S rRNA
+Macromolecule #33: mRNA
+Macromolecule #34: A-site tRNA-Pro
+Macromolecule #35: P-site tRNA-Pro
+Macromolecule #36: 23S rRNA
+Macromolecule #37: 5S rRNA
+Macromolecule #62: ZINC ION
+Macromolecule #63: MAGNESIUM ION
+Macromolecule #64: PYRROLIDINE-2-CARBALDEHYDE
+Macromolecule #65: SPERMINE
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.5 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / 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 / Nominal defocus max: 3.5 µm / Nominal defocus min: 0.5 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Keywords
Authors
Germany, 1 items
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Processing
FIELD EMISSION GUN
