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- PDB-9kcf: Bovine Flagellar TRiC -

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Basic information

Entry
Database: PDB / ID: 9kcf
TitleBovine Flagellar TRiC
Components
  • (T-complex protein 1 subunit ...) x 8
  • Probable T-complex protein 1 subunit zeta-2
KeywordsCHAPERONE / TRiC / sperm / flagella / motile cilia
Function / homology
Function and homology information


Association of TriC/CCT with target proteins during biosynthesis / RHOBTB2 GTPase cycle / RHOBTB1 GTPase cycle / 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 / Neutrophil degranulation ...Association of TriC/CCT with target proteins during biosynthesis / RHOBTB2 GTPase cycle / RHOBTB1 GTPase cycle / 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 / Neutrophil degranulation / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / WD40-repeat domain binding / chaperone-mediated protein complex assembly / Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides / beta-tubulin binding / positive regulation of telomere maintenance via telomerase / mRNA 3'-UTR binding / ATP-dependent protein folding chaperone / mRNA 5'-UTR binding / response to virus / : / melanosome / G-protein beta-subunit binding / protein folding / cell body / microtubule / protein stabilization / ubiquitin protein ligase binding / centrosome / ATP hydrolysis activity / ATP binding / metal ion binding / identical protein binding
Similarity search - Function
T-complex protein 1, alpha subunit / T-complex protein 1, eta subunit / T-complex protein 1, theta subunit / T-complex protein 1, zeta subunit / T-complex protein 1, delta subunit / T-complex protein 1, gamma subunit / T-complex protein 1, epsilon subunit / T-complex protein 1, beta subunit / : / Chaperonins TCP-1 signature 1. ...T-complex protein 1, alpha subunit / T-complex protein 1, eta subunit / T-complex protein 1, theta subunit / T-complex protein 1, zeta subunit / T-complex protein 1, delta subunit / T-complex protein 1, gamma subunit / T-complex protein 1, epsilon subunit / T-complex protein 1, beta subunit / : / Chaperonins TCP-1 signature 1. / : / Chaperonins TCP-1 signature 2. / Chaperonin TCP-1, conserved site / Chaperonins TCP-1 signature 3. / Chaperone tailless complex polypeptide 1 (TCP-1) / GroEL-like equatorial domain superfamily / TCP-1-like chaperonin intermediate domain superfamily / GroEL-like apical domain superfamily / TCP-1/cpn60 chaperonin family / Chaperonin Cpn60/GroEL/TCP-1 family
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / T-complex protein 1 subunit epsilon / T-complex protein 1 subunit eta / T-complex protein 1 subunit delta / T-complex protein 1 subunit alpha / T-complex protein 1 subunit zeta / Probable T-complex protein 1 subunit zeta-2 / T-complex protein 1 subunit gamma / T-complex protein 1 subunit beta / T-complex protein 1 subunit theta
Similarity search - Component
Biological speciesBos taurus (domestic cattle)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsCong, Y. / Meng, X.
Funding support China, 1items
OrganizationGrant numberCountry
Chinese Academy of Sciences China
CitationJournal: Mol Cell / Year: 2026
Title: Chaperonin TRiC bridges radial spokes for folding locally translated proteins to sustain mammalian sperm flagellar motility.
Authors: Xueming Meng / Luan Li / Cheng Lin / Yun Zhu / Yanyan Feng / Qun Zhao / Nan Zhao / Xuehai Zhou / Yujie Tong / Shanshan Wang / Guoliang Yin / Ruimin Liu / Lihua Zhang / Fei Sun / Xiumin Yan / ...Authors: Xueming Meng / Luan Li / Cheng Lin / Yun Zhu / Yanyan Feng / Qun Zhao / Nan Zhao / Xuehai Zhou / Yujie Tong / Shanshan Wang / Guoliang Yin / Ruimin Liu / Lihua Zhang / Fei Sun / Xiumin Yan / Xueliang Zhu / Yao Cong /
Abstract: As animals evolved from external to internal fertilization, sperm flagella, once transiently propelling sperm in water to reach nearby eggs, developed to beat for days in the viscous female ...As animals evolved from external to internal fertilization, sperm flagella, once transiently propelling sperm in water to reach nearby eggs, developed to beat for days in the viscous female reproductive tract. How flagella are remodeled accordingly remains unclear. Unlike externally fertilizing zebrafish and sea urchins, mammalian flagella feature a barrel between radial spokes (RSs) RS1 and RS2. Here, we show that this RS1-RS2 barrel (RRB) is a unique T-complex protein-1 ring complex (TRiC) that folds locally translated polypeptides to sustain flagellar motility. Cryo-electron microscopy (cryo-EM) reveals a flagellum-specific TRiC structure. An in situ cryo-electron tomography (cryo-ET) map of flagellar axonemes captures the RRB TRiC in an active, substrate-receptive state, with additional densities suggestive of folding substrates and cofactors. Mammalian flagella contain components of translation machineries and locally synthesize proteins. Cross-linking mass spectrometry identifies candidate locally translated axonemal proteins and folding substrates. Furthermore, a TRiC ATPase inhibitor markedly represses mouse sperm motility. Our findings provide insights into flagellar remodeling in internally fertilizing species.
History
DepositionNov 1, 2024Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Apr 29, 2026Provider: repository / Type: Initial release
Revision 1.0Apr 29, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Apr 29, 2026Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Apr 29, 2026Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Probable T-complex protein 1 subunit zeta-2
F: T-complex protein 1 subunit eta
H: T-complex protein 1 subunit alpha
B: T-complex protein 1 subunit beta
C: T-complex protein 1 subunit gamma
D: T-complex protein 1 subunit delta
E: T-complex protein 1 subunit epsilon
G: T-complex protein 1 subunit theta
N: T-complex protein 1 subunit eta
I: T-complex protein 1 subunit alpha
J: T-complex protein 1 subunit beta
K: T-complex protein 1 subunit gamma
L: T-complex protein 1 subunit delta
M: T-complex protein 1 subunit epsilon
O: T-complex protein 1 subunit theta
P: T-complex protein 1 subunit zeta
hetero molecules


Theoretical massNumber of molelcules
Total (without water)950,18828
Polymers947,47916
Non-polymers2,70912
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

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Protein , 1 types, 1 molecules A

#1: Protein Probable T-complex protein 1 subunit zeta-2


Mass: 58114.383 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle)
References: UniProt: Q3T084, Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides

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T-complex protein 1 subunit ... , 8 types, 15 molecules FNHIBJCKDLEMGOP

#2: Protein T-complex protein 1 subunit eta / TCP-1-eta / CCT-eta


Mass: 59518.707 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle)
References: UniProt: Q2NKZ1, Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides
#3: Protein T-complex protein 1 subunit alpha / TCP-1-alpha / CCT-alpha


Mass: 60281.312 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / Plasmid details: sperm flagella
References: UniProt: Q32L40, Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides
#4: Protein T-complex protein 1 subunit beta / TCP-1-beta / CCT-beta


Mass: 57555.188 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / Plasmid details: sperm flagella
References: UniProt: Q3ZBH0, Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides
#5: Protein T-complex protein 1 subunit gamma / TCP-1-gamma / CCT-gamma


Mass: 60666.848 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle)
References: UniProt: Q3T0K2, Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides
#6: Protein T-complex protein 1 subunit delta / TCP-1-delta / CCT-delta


Mass: 58278.355 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle)
References: UniProt: Q2T9X2, Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides
#7: Protein T-complex protein 1 subunit epsilon / CCT-epsilon


Mass: 59681.941 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: F1MWD3
#8: Protein T-complex protein 1 subunit theta / TCP-1-theta / CCT-theta


Mass: 59681.328 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: Q3ZCI9
#9: Protein T-complex protein 1 subunit zeta / TCP-1-zeta / CCT-zeta / CCT-zeta-1


Mass: 58037.086 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle)
References: UniProt: Q3MHL7, Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides

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Non-polymers , 2 types, 12 molecules

#10: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION
#11: Chemical
ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE


Mass: 427.201 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Feature type: SUBJECT OF INVESTIGATION / Comment: ADP, energy-carrying molecule*YM

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Details

Has ligand of interestY
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: TRiC purified from bovine sperm flagella / Type: COMPLEX / Entity ID: #3-#7, #9, #2, #8, #1 / Source: NATURAL
Source (natural)Organism: Bos taurus (domestic cattle)
Buffer solutionpH: 7.4
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 %

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 3000 nm / Nominal defocus min: 500 nm / Cs: 0.01 mm / C2 aperture diameter: 70 µm
Image recordingElectron dose: 54 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM software
IDNameVersionCategoryDetails (eV)
1cryoSPARC4particle selection
2RELION4particle selection
8UCSF ChimeraX1.8model fitting
10Rosetta3.14model refinement
11PHENIX1.19.2model refinementReal_space_refine module
15cryoSPARC43D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 130150 / Symmetry type: POINT
Atomic model building
IDPDB-ID 3D fitting-IDAccession codeInitial refinement model-IDSource nameType
14A0V

4a0v

14A0V1PDBexperimental model
21AF-Q3T084-F12AlphaFoldin silico model

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