[English] 日本語
![](img/lk-miru.gif)
- EMDB-32978: Cryo-EM structure of RNC-RAC complex in presence of Ssb from S. c... -
+
Open data
-
Basic information
Entry | ![]() | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Cryo-EM structure of RNC-RAC complex in presence of Ssb from S. cerevisiae 2 | |||||||||
![]() | ||||||||||
![]() |
| |||||||||
Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Chen Y / Gao N | |||||||||
Funding support | ![]()
| |||||||||
![]() | ![]() Title: Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding. Authors: Yan Chen / Bin Tsai / Ningning Li / Ning Gao / ![]() Abstract: Ribosome associated complex (RAC), an obligate heterodimer of HSP40 and HSP70 (Zuo1 and Ssz1 in yeast), is conserved in eukaryotes and functions as co-chaperone for another HSP70 (Ssb1/2 in yeast) to ...Ribosome associated complex (RAC), an obligate heterodimer of HSP40 and HSP70 (Zuo1 and Ssz1 in yeast), is conserved in eukaryotes and functions as co-chaperone for another HSP70 (Ssb1/2 in yeast) to facilitate co-translational folding of nascent polypeptides. Many mechanistic details, such as the coordination of one HSP40 with two HSP70s and the dynamic interplay between RAC-Ssb and growing nascent chains, remain unclear. Here, we report three sets of structures of RAC-containing ribosomal complexes isolated from Saccharomyces cerevisiae. Structural analyses indicate that RAC on the nascent-chain-free ribosome is in an autoinhibited conformation, and in the presence of a nascent chain at the peptide tunnel exit (PTE), RAC undergoes large-scale structural remodeling to make Zuo1 J-Domain more accessible to Ssb. Our data also suggest a role of Zuo1 in orienting Ssb-SBD proximal to the PTE for easy capture of the substrate. Altogether, in accordance with previous data, our work suggests a sequence of structural remodeling events for RAC-Ssb during co-translational folding, triggered by the binding and passage of growing nascent chain from one to another. | |||||||||
History |
|
-
Structure visualization
Supplemental images |
---|
-
Downloads & links
-EMDB archive
Map data | ![]() | 140.2 MB | ![]() | |
---|---|---|---|---|
Header (meta data) | ![]() ![]() | 14.2 KB 14.2 KB | Display Display | ![]() |
Images | ![]() | 70.3 KB | ||
Others | ![]() ![]() | 140.9 MB 140.8 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7x34MC ![]() 7x3kC M: atomic model generated by this map C: citing same article ( |
---|---|
Similar structure data | Similarity search - Function & homology ![]() |
-
Links
EMDB pages | ![]() ![]() |
---|---|
Related items in Molecule of the Month |
-
Map
File | ![]() | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Voxel size | X=Y=Z: 1.356 Å | ||||||||||||||||||||
Density |
| ||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
|
-Supplemental data
-Half map: #2
File | emd_32978_half_map_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: #1
File | emd_32978_half_map_2.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-
Sample components
-Entire : RNC-RAC complex in presence of Ssb from S. cerevisiae 2
Entire | Name: RNC-RAC complex in presence of Ssb from S. cerevisiae 2 |
---|---|
Components |
|
-Supramolecule #1: RNC-RAC complex in presence of Ssb from S. cerevisiae 2
Supramolecule | Name: RNC-RAC complex in presence of Ssb from S. cerevisiae 2 type: complex / Chimera: Yes / ID: 1 / Parent: 0 / Macromolecule list: all |
---|---|
Source (natural) | Organism: ![]() ![]() ![]() |
Recombinant expression | Organism: ![]() ![]() ![]() |
-Macromolecule #1: Zuotin
Macromolecule | Name: Zuotin / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() ![]() ![]() |
Molecular weight | Theoretical: 10.619055 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: ASAKADKKKA KEAAKAAKKK NKRAIRNSAK EADYFGDADK ATTIDEQVGL IVDSLNDEEL VSTADKIKAN AAGAKEVLKE SAKTIVDSG KLPSSLLSYF V |
-Macromolecule #2: RNA (130-mer)
Macromolecule | Name: RNA (130-mer) / type: rna / ID: 2 / Number of copies: 1 |
---|---|
Source (natural) | Organism: ![]() ![]() ![]() |
Molecular weight | Theoretical: 42.010996 KDa |
Sequence | String: CGCCCGUCGC UAGUACCGAU UGAAUGGCUU AGUGAGGCCU CAGGAUCUGC UUAGAGAAGG GGGCAACUCC AUCUCAGAGC GGAGAAUUU GGACAAACUU GGUCAUUUAG AGGAACUAAA AGUCGUAACA A |
-Experimental details
-Structure determination
Method | ![]() ![]() |
---|---|
![]() | ![]() |
Aggregation state | particle |
-
Sample preparation
Buffer | pH: 7.4 |
---|---|
Staining | Type: NEGATIVE / Material: Uranyl Acetate |
Vitrification | Cryogen name: NITROGEN |
-
Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: DARK FIELD / Nominal defocus max: 1.6 µm / Nominal defocus min: 1.0 µm |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 35.0 e/Å2 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
-
Image processing
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
---|---|
Final angle assignment | Type: MAXIMUM LIKELIHOOD |
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 65816 |
-Atomic model buiding 1
Refinement | Protocol: RIGID BODY FIT |
---|---|
Output model | ![]() PDB-7x34: |