- EMDB-4300: Structure of a prehandover mammalian ribosomal SRP and SRP recept... -
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Basic information
Entry
Database: EMDB / ID: EMD-4300
Title
Structure of a prehandover mammalian ribosomal SRP and SRP receptor targeting complex
Map data
Sample
Complex: Translating ribosome bound to SRP and SRP receptor
Complex: Ribosome
RNA: x 4 types
Protein or peptide: x 45 types
Complex: SRP
RNA: x 1 types
Protein or peptide: x 6 types
Complex: SRP receptor
Protein or peptide: x 2 types
Complex: Signal sequence
Ligand: x 4 types
Function / homology
Function and homology information
SRP-dependent cotranslational protein targeting to membrane / signal recognition particle receptor complex / SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition / endoplasmic reticulum signal peptide binding / signal recognition particle, endoplasmic reticulum targeting / granulocyte differentiation / signal recognition particle binding / protein localization to Golgi apparatus / protein targeting to ER / signal-recognition-particle GTPase ...SRP-dependent cotranslational protein targeting to membrane / signal recognition particle receptor complex / SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition / endoplasmic reticulum signal peptide binding / signal recognition particle, endoplasmic reticulum targeting / granulocyte differentiation / signal recognition particle binding / protein localization to Golgi apparatus / protein targeting to ER / signal-recognition-particle GTPase / negative regulation of translational elongation / SRP-dependent cotranslational protein targeting to membrane, translocation / Golgi to plasma membrane protein transport / 7S RNA binding / exocrine pancreas development / SRP-dependent cotranslational protein targeting to membrane / TPR domain binding / ribonucleoprotein complex binding / cytoplasmic microtubule / neutrophil chemotaxis / intracellular protein transport / GDP binding / ribosome binding / nuclear speck / GTPase activity / endoplasmic reticulum membrane / nucleolus / GTP binding / Golgi apparatus / endoplasmic reticulum / ATP hydrolysis activity / nucleoplasm / nucleus / cytosol Similarity search - Function
Signal recognition particle receptor, alpha subunit, N-terminal / Signal recognition particle, alpha subunit, N-terminal / Signal recognition particle receptor, beta subunit / Signal recognition particle receptor beta subunit / Signal recognition particle, SRP72 subunit, RNA-binding / Signal recognition particle, SRP72 subunit / Putative TPR-like repeat / SRP72 RNA-binding domain / Putative TPR-like repeat / Signal recognition particle, SRP9 subunit ...Signal recognition particle receptor, alpha subunit, N-terminal / Signal recognition particle, alpha subunit, N-terminal / Signal recognition particle receptor, beta subunit / Signal recognition particle receptor beta subunit / Signal recognition particle, SRP72 subunit, RNA-binding / Signal recognition particle, SRP72 subunit / Putative TPR-like repeat / SRP72 RNA-binding domain / Putative TPR-like repeat / Signal recognition particle, SRP9 subunit / SRP9 domain / Signal recognition particle SRP9 / Signal recognition particle 9 kDa protein (SRP9) / Signal recognition particle, SRP14 subunit / Signal recognition particle, SRP9/SRP14 subunit / Signal recognition particle 14kD protein / Signal recognition particle subunit SRP68 / Signal recognition particle subunit SRP68, RNA-binding domain / SRP68, N-terminal domain superfamily / RNA-binding signal recognition particle 68 / Signal recognition particle, SRP54 subunit, eukaryotic / Signal recognition particle, SRP19 subunit / Signal recognition particle, subunit SRP19-like superfamily / SRP19 protein / SRP/SRP receptor, N-terminal / Signal recognition particle, SRP54 subunit / Signal recognition particle, SRP54 subunit, M-domain / Signal recognition particle, SRP54 subunit, M-domain superfamily / Signal peptide binding domain / SRP54-type proteins GTP-binding domain signature. / Signal recognition particle SRP54, helical bundle / Signal recognition particle SRP54, N-terminal domain superfamily / SRP54-type protein, helical bundle domain / SRP54-type protein, helical bundle domain / Signal recognition particle, SRP54 subunit, GTPase domain / SRP54-type protein, GTPase domain / SRP54-type protein, GTPase domain / Small GTPase superfamily, ARF type / small GTPase Arf family profile. / Longin-like domain superfamily / Tetratricopeptide repeat / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Tetratricopeptide-like helical domain superfamily / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase Similarity search - Domain/homology
Signal recognition particle receptor subunit beta / SRP receptor subunit alpha / Signal recognition particle 19 kDa protein / Signal recognition particle 14 kDa protein / Signal recognition particle 9 kDa protein / Signal recognition particle subunit SRP72 / Signal recognition particle subunit SRP54 / Signal recognition particle subunit SRP68 Similarity search - Component
Journal: Science / Year: 2018 Title: Structure of a prehandover mammalian ribosomal SRP·SRP receptor targeting complex. Authors: Kan Kobayashi / Ahmad Jomaa / Jae Ho Lee / Sowmya Chandrasekar / Daniel Boehringer / Shu-Ou Shan / Nenad Ban / Abstract: Signal recognition particle (SRP) targets proteins to the endoplasmic reticulum (ER). SRP recognizes the ribosome synthesizing a signal sequence and delivers it to the SRP receptor (SR) on the ER ...Signal recognition particle (SRP) targets proteins to the endoplasmic reticulum (ER). SRP recognizes the ribosome synthesizing a signal sequence and delivers it to the SRP receptor (SR) on the ER membrane followed by the transfer of the signal sequence to the translocon. Here, we present the cryo-electron microscopy structure of the mammalian translating ribosome in complex with SRP and SR in a conformation preceding signal sequence handover. The structure visualizes all eukaryotic-specific SRP and SR proteins and reveals their roles in stabilizing this conformation by forming a large protein assembly at the distal site of SRP RNA. We provide biochemical evidence that the guanosine triphosphate hydrolysis of SRP·SR is delayed at this stage, possibly to provide a time window for signal sequence handover to the translocon.
History
Deposition
Feb 16, 2018
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Header (metadata) release
Mar 28, 2018
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Map release
Mar 28, 2018
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Update
May 2, 2018
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Current status
May 2, 2018
Processing site: PDBe / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
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