[English] 日本語
Yorodumi- PDB-4b2t: The crystal structures of the eukaryotic chaperonin CCT reveal it... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4b2t | ||||||
---|---|---|---|---|---|---|---|
Title | The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning | ||||||
Components | (T-COMPLEX PROTEIN 1 SUBUNIT ...) x 8 | ||||||
Keywords | CHAPERONE | ||||||
Function / homology | Function and homology information BBSome-mediated cargo-targeting to cilium / Association of TriC/CCT with target proteins during biosynthesis / RHOBTB1 GTPase cycle / RHOBTB2 GTPase cycle / : / zona pellucida receptor complex / scaRNA localization to Cajal body / chaperone mediated protein folding independent of cofactor / positive regulation of establishment of protein localization to telomere / chaperonin-containing T-complex ...BBSome-mediated cargo-targeting to cilium / Association of TriC/CCT with target proteins during biosynthesis / RHOBTB1 GTPase cycle / RHOBTB2 GTPase cycle / : / zona pellucida receptor complex / scaRNA localization to Cajal body / chaperone mediated protein folding independent of cofactor / positive regulation of establishment of protein localization to telomere / chaperonin-containing T-complex / positive regulation of telomerase RNA localization to Cajal body / binding of sperm to zona pellucida / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / Neutrophil degranulation / beta-tubulin binding / chaperone-mediated protein complex assembly / chaperone-mediated protein folding / positive regulation of telomere maintenance via telomerase / mRNA 3'-UTR binding / ATP-dependent protein folding chaperone / response to virus / mRNA 5'-UTR binding / cilium / G-protein beta-subunit binding / melanosome / unfolded protein binding / protein folding / cell body / microtubule / protein stabilization / centrosome / ubiquitin protein ligase binding / ATP hydrolysis activity / ATP binding Similarity search - Function | ||||||
Biological species | BOS TAURUS (cattle) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 5.5 Å | ||||||
Authors | Kalisman, N. / Schroeder, G.F. / Levitt, M. | ||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2011 Title: Crystal Structure of the Open Conformation of the Mammalian Chaperonin Cct in Complex with Tubulin. Authors: Munoz, I.G. / Yebenes, H. / Zhou, M. / Mesa, P. / Serna, M. / Park, A.Y. / Bragado-Nilsson, E. / Beloso, A. / De Carcer, G. / Malumbres, M. / Robinson, C.V. / Valpuesta, J.M. / Montoya, G. | ||||||
History |
| ||||||
Remark 0 | THIS ENTRY 4B2T REFLECTS AN ALTERNATIVE MODELING OF THE ORIGINAL STRUCTURAL DATA (R2XSMSF) ...THIS ENTRY 4B2T REFLECTS AN ALTERNATIVE MODELING OF THE ORIGINAL STRUCTURAL DATA (R2XSMSF) DETERMINED BY AUTHORS OF THE PDB ENTRY 2XSM: I.G.MUNOZ,H.YEBENES,M.ZHOU,P.MESA,M.SERNA,E.BRAGADO-NILSSON, A.BELOSO,C.V.ROBINSON,J.M.VALPUESTA,G.MONTOYA |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 4b2t.cif.gz | 1.1 MB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb4b2t.ent.gz | 909.3 KB | Display | PDB format |
PDBx/mmJSON format | 4b2t.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b2/4b2t ftp://data.pdbj.org/pub/pdb/validation_reports/b2/4b2t | HTTPS FTP |
---|
-Related structure data
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
-T-COMPLEX PROTEIN 1 SUBUNIT ... , 8 types, 16 molecules AaBbDdEeGgHhQqZz
#1: Protein | Mass: 60281.312 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: TESTES / References: UniProt: Q32L40 #2: Protein | Mass: 57555.188 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: TESTES / References: UniProt: Q3ZBH0 #3: Protein | Mass: 58233.402 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: TESTES / References: UniProt: Q2T9X2 #4: Protein | Mass: 59695.965 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: TESTES / References: UniProt: F1MWD3*PLUS #5: Protein | Mass: 60666.848 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: TESTES / References: UniProt: Q3T0K2 #6: Protein | Mass: 59518.707 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: TESTES / References: UniProt: Q2NKZ1 #7: Protein | Mass: 59681.328 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: TESTES / References: UniProt: Q3ZCI9 #8: Protein | Mass: 58037.086 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: TESTES / References: UniProt: Q3MHL7 |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 4.66 Å3/Da / Density % sol: 73.38 % / Description: AUTHOR USED THE SF DATA FROM ENTRY 2XSM. |
---|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1.114 Å |
Detector | Type: PSI PILATUS 6M / Detector: PIXEL / Date: Oct 15, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.114 Å / Relative weight: 1 |
-Processing
Software | Name: CNS / Version: 1.3 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 5.5→200 Å / Data cutoff high absF: 10000 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: MLF
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Solvent model: FLAT MODEL / Bsol: 228.728 Å2 / ksol: 0.3 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 277.1 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 5.5→200 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 5.5→5.7 Å / Total num. of bins used: 10
|