+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-31173 | |||||||||
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Title | CrClpP-S2c | |||||||||
Map data | The 3.6 angstrom resolution cryo-EM density map of CrClp-cpn11/20/23 complex in Chlamydomonas reinhardtii. | |||||||||
Sample |
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Function / homology | Function and homology information endopeptidase Clp complex / endopeptidase Clp / plastid / chloroplast stroma / ATP-dependent peptidase activity / protein quality control for misfolded or incompletely synthesized proteins / chaperone cofactor-dependent protein refolding / chloroplast / unfolded protein binding / ATPase binding ...endopeptidase Clp complex / endopeptidase Clp / plastid / chloroplast stroma / ATP-dependent peptidase activity / protein quality control for misfolded or incompletely synthesized proteins / chaperone cofactor-dependent protein refolding / chloroplast / unfolded protein binding / ATPase binding / protein-folding chaperone binding / mitochondrial matrix / serine-type endopeptidase activity / ATP hydrolysis activity / ATP binding / metal ion binding Similarity search - Function | |||||||||
Biological species | Chlamydomonas reinhardtii (plant) / Chlamydomonas smithii (plant) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.6 Å | |||||||||
Authors | Wang N / Wang YF / Cong Y / Liu CM | |||||||||
Citation | Journal: Nat Plants / Year: 2021 Title: The cryo-EM structure of the chloroplast ClpP complex. Authors: Ning Wang / Yifan Wang / Qian Zhao / Xiang Zhang / Chao Peng / Wenjuan Zhang / Yanan Liu / Olivier Vallon / Michael Schroda / Yao Cong / Cuimin Liu / Abstract: Protein homoeostasis in plastids is strategically regulated by the protein quality control system involving multiple chaperones and proteases, among them the Clp protease. Here, we determined the ...Protein homoeostasis in plastids is strategically regulated by the protein quality control system involving multiple chaperones and proteases, among them the Clp protease. Here, we determined the structure of the chloroplast ClpP complex from Chlamydomonas reinhardtii by cryo-electron microscopy. ClpP contains two heptameric catalytic rings without any symmetry. The top ring contains one ClpR6, three ClpP4 and three ClpP5 subunits while the bottom ring is composed of three ClpP1 subunits and one each of the ClpR1-4 subunits. ClpR3, ClpR4 and ClpT4 subunits connect the two rings and stabilize the complex. The chloroplast Cpn11/20/23 co-chaperonin, a co-factor of Cpn60, forms a cap on the top of ClpP by protruding mobile loops into hydrophobic clefts at the surface of the top ring. The co-chaperonin repressed ClpP proteolytic activity in vitro. By regulating Cpn60 chaperone and ClpP protease activity, the co-chaperonin may play a role in coordinating protein folding and degradation in the chloroplast. | |||||||||
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_31173.map.gz | 1.8 MB | EMDB map data format | |
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Header (meta data) | emd-31173-v30.xml emd-31173.xml | 20.6 KB 20.6 KB | Display Display | EMDB header |
Images | emd_31173.png | 70.8 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-31173 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-31173 | HTTPS FTP |
-Related structure data
Related structure data | 7ekqMC 7ekoC 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_31173.map.gz / Format: CCP4 / Size: 38.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | The 3.6 angstrom resolution cryo-EM density map of CrClp-cpn11/20/23 complex in Chlamydomonas reinhardtii. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.318 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 : complex of CrClp protease and co-chaperonin Cpn112023
+Supramolecule #1: complex of CrClp protease and co-chaperonin Cpn112023
+Macromolecule #1: ATP-dependent Clp protease proteolytic subunit
+Macromolecule #2: ATP-dependent Clp protease proteolytic subunit
+Macromolecule #3: ATP-dependent Clp protease proteolytic subunit
+Macromolecule #4: ATP-dependent Clp protease proteolytic subunit
+Macromolecule #5: ATP-dependent Clp protease proteolytic subunit
+Macromolecule #6: ATP-dependent Clp protease proteolytic subunit
+Macromolecule #7: ATP-dependent Clp protease proteolytic subunit
+Macromolecule #8: ATP-dependent Clp protease proteolytic subunit
+Macromolecule #9: ATP-dependent Clp protease ATP-binding subunit CLPT4, chloroplastic
+Macromolecule #10: Chaperonin 11
+Macromolecule #11: Chaperonin 23
+Macromolecule #12: Cpn20 co-chaperonin subunit
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 Component:
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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 |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 38.0 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Initial angle assignment | Type: ANGULAR RECONSTITUTION |
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Final angle assignment | Type: ANGULAR RECONSTITUTION |
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 49759 |