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Open data
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Basic information
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| Title | mouse PDCD5-TRiC complex | |||||||||
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Keywords | Complex / cofactor / CHAPERONE | |||||||||
| Function / homology | Function and homology informationAssociation of TriC/CCT with target proteins during biosynthesis / RHOBTB1 GTPase cycle / negative regulation of protein folding / RHOBTB2 GTPase cycle / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / zona pellucida receptor complex / positive regulation of establishment of protein localization to telomere / scaRNA localization to Cajal body / positive regulation of telomerase RNA localization to Cajal body / chaperonin-containing T-complex ...Association of TriC/CCT with target proteins during biosynthesis / RHOBTB1 GTPase cycle / negative regulation of protein folding / RHOBTB2 GTPase cycle / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / zona pellucida receptor complex / positive regulation of establishment of protein localization to telomere / scaRNA localization to Cajal body / positive regulation of telomerase RNA localization to Cajal body / chaperonin-containing T-complex / binding of sperm to zona pellucida / acetyltransferase activator activity / WD40-repeat domain binding / pericentriolar material / microtubule organizing center / cellular response to transforming growth factor beta stimulus / chaperone-mediated protein complex assembly / Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides / beta-tubulin binding / heterochromatin / positive regulation of telomere maintenance via telomerase / Neutrophil degranulation / protein folding chaperone / acrosomal vesicle / mRNA 3'-UTR binding / ATP-dependent protein folding chaperone / mRNA 5'-UTR binding / response to virus / melanosome / unfolded protein binding / myelin sheath / heparin binding / G-protein beta-subunit binding / protein folding / cell body / regulation of apoptotic process / microtubule / protein stabilization / positive regulation of apoptotic process / apoptotic process / ubiquitin protein ligase binding / positive regulation of gene expression / centrosome / Golgi apparatus / ATP hydrolysis activity / mitochondrion / DNA binding / nucleoplasm / ATP binding / metal ion binding / identical protein binding / nucleus / cytoplasm / cytosol Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.55 Å | |||||||||
Authors | Song QQ / Cong Y | |||||||||
| Funding support | China, 1 items
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Citation | Journal: Mol Cell / Year: 2026Title: PDCD5 promotes substrate release from the TRiC complex in cilia and flagella. Authors: Huafang Wei / Qianqian Song / Liying Wang / Qiong Deng / Bingbing Wu / Yinghong Chen / Tingting Han / Yueshuai Guo / Zuyang Li / Fucheng Dong / Shuang Ma / Qiaoyu Zhao / Xiangyi Shi / Chen ...Authors: Huafang Wei / Qianqian Song / Liying Wang / Qiong Deng / Bingbing Wu / Yinghong Chen / Tingting Han / Yueshuai Guo / Zuyang Li / Fucheng Dong / Shuang Ma / Qiaoyu Zhao / Xiangyi Shi / Chen Pan / Wanying Jiang / Xiaofei Liu / Yingyu Chen / Renjie Jiao / Li Yuan / Chao Liu / Xuejiang Guo / Yao Cong / Wei Li / ![]() Abstract: Approximately 10% of eukaryotic proteins are folded by the TRiC/CCT complex (TCP1-ring complex, also called CCT for cytosolic chaperonin containing TCP1), and only open-state TRiC can bind with ...Approximately 10% of eukaryotic proteins are folded by the TRiC/CCT complex (TCP1-ring complex, also called CCT for cytosolic chaperonin containing TCP1), and only open-state TRiC can bind with programmed cell death 5 (PDCD5). However, the physiological role of the PDCD5-TRiC interaction remains elusive. Here, we show that PDCD5 is required for flagellum biogenesis and ciliogenesis and present the PDCD5-TRiC structures in their open states at near-atomic resolution. Mechanically, we find that PDCD5 promotes substrates release by competing with PhLP2A to interact with TRiC, and the depletion of PDCD5 traps flagellum- and cilium-associated proteins within TRiC, finally leading to malformed flagella of spermatids and cilia in mouse ciliated cells. Moreover, we demonstrate that the function of PDCD5 in flagellum biogenesis and ciliogenesis depends on the interaction with TRiC by its C terminus. These findings identify PDCD5 as a TRiC regulator to promote a subset of proteins release. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_64367.map.gz | 10.8 MB | EMDB map data format | |
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| Header (meta data) | emd-64367-v30.xml emd-64367.xml | 23.1 KB 23.1 KB | Display Display | EMDB header |
| Images | emd_64367.png | 73.2 KB | ||
| Filedesc metadata | emd-64367.cif.gz | 8.8 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-64367 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-64367 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9unwMC 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_64367.map.gz / Format: CCP4 / Size: 244.1 MB / 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: 0.87 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 : mouse PDCD5-TRiC complex
+Supramolecule #1: mouse PDCD5-TRiC complex
+Macromolecule #1: T-complex protein 1 subunit alpha
+Macromolecule #2: T-complex protein 1 subunit beta
+Macromolecule #3: T-complex protein 1 subunit gamma
+Macromolecule #4: T-complex protein 1 subunit delta
+Macromolecule #5: T-complex protein 1 subunit epsilon
+Macromolecule #6: T-complex protein 1 subunit zeta
+Macromolecule #7: T-complex protein 1 subunit eta
+Macromolecule #8: T-complex protein 1 subunit theta
+Macromolecule #9: Programmed cell death protein 5
-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: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 57.0 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: 15.0 µm / Nominal defocus min: 9.0 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Authors
China, 1 items
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Processing
FIELD EMISSION GUN

