+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-12801 | |||||||||
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Title | RNC-SRP early complex | |||||||||
Map data | RNC-SRP complex | |||||||||
Sample |
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Keywords | SRP SRP receptor / co-translational protein targeting / endoplasmic reticulum / signal peptide / RNA BINDING PROTEIN | |||||||||
Function / homology | Function and homology information PI3K Cascade / PIP3 activates AKT signaling / FLT3 Signaling / Negative regulation of FLT3 / FLT3 signaling through SRC family kinases / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / RAF/MAP kinase cascade / SRP-dependent cotranslational protein targeting to membrane / SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition / endoplasmic reticulum signal peptide binding ...PI3K Cascade / PIP3 activates AKT signaling / FLT3 Signaling / Negative regulation of FLT3 / FLT3 signaling through SRC family kinases / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / RAF/MAP kinase cascade / SRP-dependent cotranslational protein targeting to membrane / SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition / endoplasmic reticulum signal peptide binding / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / Hydrolases; Acting on peptide bonds (peptidases); Dipeptidyl-peptidases and tripeptidyl-peptidases / signal recognition particle, endoplasmic reticulum targeting / Translesion synthesis by REV1 / Recognition of DNA damage by PCNA-containing replication complex / Translesion Synthesis by POLH / Downregulation of ERBB4 signaling / Spry regulation of FGF signaling / Downregulation of ERBB2:ERBB3 signaling / NOD1/2 Signaling Pathway / APC/C:Cdc20 mediated degradation of Cyclin B / APC-Cdc20 mediated degradation of Nek2A / EGFR downregulation / TCF dependent signaling in response to WNT / NRIF signals cell death from the nucleus / p75NTR recruits signalling complexes / NF-kB is activated and signals survival / Activated NOTCH1 Transmits Signal to the Nucleus / Downregulation of TGF-beta receptor signaling / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / Downregulation of SMAD2/3:SMAD4 transcriptional activity / SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription / Senescence-Associated Secretory Phenotype (SASP) / Regulation of innate immune responses to cytosolic DNA / activated TAK1 mediates p38 MAPK activation / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / Regulation of FZD by ubiquitination / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Regulation of TNFR1 signaling / TNFR1-induced NF-kappa-B signaling pathway / Translesion synthesis by POLK / Translesion synthesis by POLI / Regulation of necroptotic cell death / HDR through Homologous Recombination (HRR) / Josephin domain DUBs / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / Processing of DNA double-strand break ends / Formation of Incision Complex in GG-NER / Gap-filling DNA repair synthesis and ligation in GG-NER / Dual Incision in GG-NER / Fanconi Anemia Pathway / Regulation of TP53 Activity through Phosphorylation / Regulation of TP53 Degradation / Regulation of TP53 Activity through Methylation / Negative regulation of MET activity / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Downregulation of ERBB2 signaling / E3 ubiquitin ligases ubiquitinate target proteins / Regulation of PTEN localization / ER Quality Control Compartment (ERQC) / Regulation of expression of SLITs and ROBOs / Interferon alpha/beta signaling / Endosomal Sorting Complex Required For Transport (ESCRT) / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / IKK complex recruitment mediated by RIP1 / IRAK2 mediated activation of TAK1 complex / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Alpha-protein kinase 1 signaling pathway / RAS processing / Pexophagy / Negative regulation of FLT3 / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / Regulation of NF-kappa B signaling / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / Regulation of pyruvate metabolism / SCF-beta-TrCP mediated degradation of Emi1 / Termination of translesion DNA synthesis / MAP3K8 (TPL2)-dependent MAPK1/3 activation / Ovarian tumor domain proteases / Cyclin D associated events in G1 / Negative regulators of DDX58/IFIH1 signaling / Regulation of BACH1 activity / Negative regulation of FGFR1 signaling / Negative regulation of FGFR2 signaling / Negative regulation of FGFR3 signaling / Negative regulation of FGFR4 signaling / Negative regulation of MAPK pathway / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Inactivation of CSF3 (G-CSF) signaling / Iron uptake and transport / Deactivation of the beta-catenin transactivating complex / Metalloprotease DUBs / Formation of TC-NER Pre-Incision Complex / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / Major pathway of rRNA processing in the nucleolus and cytosol / GTP hydrolysis and joining of the 60S ribosomal subunit / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 Similarity search - Function | |||||||||
Biological species | Oryctolagus cuniculus (rabbit) / Canis lupus familiaris (dog) / Saccharomyces cerevisiae (brewer's yeast) / Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.8 Å | |||||||||
Authors | Jomaa A / Ban N | |||||||||
Funding support | Switzerland, 1 items
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Citation | Journal: Cell Rep / Year: 2021 Title: Molecular mechanism of cargo recognition and handover by the mammalian signal recognition particle. Authors: Ahmad Jomaa / Simon Eitzinger / Zikun Zhu / Sowmya Chandrasekar / Kan Kobayashi / Shu-Ou Shan / Nenad Ban / Abstract: Co-translational protein targeting to membranes by the signal recognition particle (SRP) is a universally conserved pathway from bacteria to humans. In mammals, SRP and its receptor (SR) have many ...Co-translational protein targeting to membranes by the signal recognition particle (SRP) is a universally conserved pathway from bacteria to humans. In mammals, SRP and its receptor (SR) have many additional RNA features and protein components compared to the bacterial system, which were recently shown to play regulatory roles. Due to its complexity, the mammalian SRP targeting process is mechanistically not well understood. In particular, it is not clear how SRP recognizes translating ribosomes with exposed signal sequences and how the GTPase activity of SRP and SR is regulated. Here, we present electron cryo-microscopy structures of SRP and SRP·SR in complex with the translating ribosome. The structures reveal the specific molecular interactions between SRP and the emerging signal sequence and the elements that regulate GTPase activity of SRP·SR. Our results suggest the molecular mechanism of how eukaryote-specific elements regulate the early and late stages of SRP-dependent protein targeting. #1: Journal: Cell Rep / Year: 2021 Title: Molecular mechanism of cargo recognition and handover by the mammalian signal recognition particle Authors: Jomaa A / Eitzinger S / Zhu Z / Chandrasekar S / Kobayashi K / Shan S / Ban N | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_12801.map.gz | 322 MB | EMDB map data format | |
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Header (meta data) | emd-12801-v30.xml emd-12801.xml | 76.3 KB 76.3 KB | Display Display | EMDB header |
Images | emd_12801.png | 143.6 KB | ||
Filedesc metadata | emd-12801.cif.gz | 15.6 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-12801 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-12801 | HTTPS FTP |
-Validation report
Summary document | emd_12801_validation.pdf.gz | 709.2 KB | Display | EMDB validaton report |
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Full document | emd_12801_full_validation.pdf.gz | 708.8 KB | Display | |
Data in XML | emd_12801_validation.xml.gz | 7.3 KB | Display | |
Data in CIF | emd_12801_validation.cif.gz | 8.5 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-12801 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-12801 | HTTPS FTP |
-Related structure data
Related structure data | 7obrMC 7obqC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_12801.map.gz / Format: CCP4 / Size: 343 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | RNC-SRP complex | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.07 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
+Entire : RNC-SRP complex
+Supramolecule #1: RNC-SRP complex
+Supramolecule #2: RNC-SRP complex
+Supramolecule #3: RNC-SRP complex
+Supramolecule #4: polypeptide nascent chain
+Macromolecule #1: SRP RNA
+Macromolecule #2: 28S rRNA
+Macromolecule #3: 5S ribosomal RNA
+Macromolecule #4: 5.8S ribosomal RNA
+Macromolecule #5: 60S ribosomal protein L8
+Macromolecule #6: uL3
+Macromolecule #7: 60S ribosomal protein L4
+Macromolecule #8: 60S ribosomal protein L5
+Macromolecule #9: 60S ribosomal protein L6
+Macromolecule #10: uL30
+Macromolecule #11: 60S ribosomal protein L7a
+Macromolecule #12: 60S ribosomal protein L9
+Macromolecule #13: 60S ribosomal protein L10
+Macromolecule #14: Ribosomal protein L11
+Macromolecule #15: 60S ribosomal protein L13
+Macromolecule #16: 60S ribosomal protein L14
+Macromolecule #17: Ribosomal protein L15
+Macromolecule #18: 60S ribosomal protein L13a
+Macromolecule #19: uL22
+Macromolecule #20: eL18
+Macromolecule #21: 60S RIBOSOMAL PROTEIN EL19
+Macromolecule #22: 60S ribosomal protein L18a
+Macromolecule #23: eL21
+Macromolecule #24: Ribosomal protein L22
+Macromolecule #25: Ribosomal protein L23
+Macromolecule #26: Ribosomal protein L24
+Macromolecule #27: uL23
+Macromolecule #28: Ribosomal protein L26
+Macromolecule #29: 60S ribosomal protein L27
+Macromolecule #30: uL15
+Macromolecule #31: 60S ribosomal protein L29
+Macromolecule #32: 60S ribosomal protein L30
+Macromolecule #33: eL31
+Macromolecule #34: eL32
+Macromolecule #35: eL33
+Macromolecule #36: 60S ribosomal protein L34
+Macromolecule #37: uL29
+Macromolecule #38: 60S ribosomal protein L36
+Macromolecule #39: Ribosomal protein L37
+Macromolecule #40: eL38
+Macromolecule #41: eL39
+Macromolecule #42: 60S RIBOSOMAL PROTEIN EL40
+Macromolecule #43: 60s ribosomal protein l41
+Macromolecule #44: eL42
+Macromolecule #45: eL43
+Macromolecule #46: Signal recognition particle 19
+Macromolecule #47: eL28
+Macromolecule #48: Dipeptidyl aminopeptidase B
+Macromolecule #49: Signal recognition particle 14 kDa protein
+Macromolecule #50: Signal recognition particle subunit SRP68
+Macromolecule #51: Signal recognition particle 9 kDa protein
+Macromolecule #52: Signal recognition particle 54 kDa protein
+Macromolecule #53: Signal recognition particle subunit SRP72
+Macromolecule #54: MAGNESIUM ION
+Macromolecule #55: ZINC ION
+Macromolecule #56: GUANOSINE-5'-DIPHOSPHATE
-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: Quantifoil R2/2 / Support film - Material: CARBON |
Vitrification | Cryogen name: ETHANE-PROPANE |
-Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 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: OTHER / Details: From initial reconstruction |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 2.8 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 43135 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD / Software - Name: RELION |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |