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- PDB-3j1c: Cryo-EM structure of 9-fold symmetric rATcpn-alpha in apo state -

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Basic information

Entry
Database: PDB / ID: 3j1c
TitleCryo-EM structure of 9-fold symmetric rATcpn-alpha in apo state
ComponentsChaperonin alpha subunit
KeywordsCHAPERONE / Group II chaperonin
Function / homology
Function and homology information


ATP-dependent protein folding chaperone / unfolded protein binding / ATP hydrolysis activity / ATP binding
Similarity search - Function
Thermosome, archaeal / 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 ...Thermosome, archaeal / 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
Chaperonin alpha subunit
Similarity search - Component
Biological speciesAcidianus tengchongensis (archaea)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 9.1 Å
AuthorsZhang, K. / Wang, L. / Liu, Y.X. / Wang, X. / Gao, B. / Hu, Z.J. / Ji, G. / Chan, K.Y. / Schulten, K. / Dong, Z.Y. / Sun, F.
CitationJournal: Protein Cell / Year: 2013
Title: Flexible interwoven termini determine the thermal stability of thermosomes.
Authors: Kai Zhang / Li Wang / Yanxin Liu / Kwok-Yan Chan / Xiaoyun Pang / Klaus Schulten / Zhiyang Dong / Fei Sun /
Abstract: Group II chaperonins, which assemble as double-ring complexes, assist in the refolding of nascent peptides or denatured proteins in an ATP-dependent manner. The molecular mechanism of group II ...Group II chaperonins, which assemble as double-ring complexes, assist in the refolding of nascent peptides or denatured proteins in an ATP-dependent manner. The molecular mechanism of group II chaperonin assembly and thermal stability is yet to be elucidated. Here, we selected the group II chaperonins (cpn-α and cpn-β), also called thermosomes, from Acidianus tengchongensis and investigated their assembly and thermal stability. We found that the binding of ATP or its analogs contributed to the successful assembly of thermosomes and enhanced their thermal stabilities. Cpn-β is more thermally stable than cpn-α, while the thermal stability of the hetero thermosome cpn-αβ is intermediate. Cryo-electron microscopy reconstructions of cpn-α and cpn-β revealed the interwoven densities of their non-conserved flexible N/C-termini around the equatorial planes. The deletion or swapping of their termini and pH-dependent thermal stability assays revealed the key role of the termini electrostatic interactions in the assembly and thermal stability of the thermosomes.
History
DepositionFeb 6, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 7, 2013Provider: repository / Type: Initial release
Revision 1.1Jul 18, 2018Group: Data collection / Category: em_software / Item: _em_software.image_processing_id
Revision 1.2Feb 21, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / em_3d_fitting_list / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _em_3d_fitting_list.accession_code / _em_3d_fitting_list.initial_refinement_model_id / _em_3d_fitting_list.source_name / _em_3d_fitting_list.type

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Structure visualization

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Assembly

Deposited unit
A: Chaperonin alpha subunit
B: Chaperonin alpha subunit
C: Chaperonin alpha subunit
D: Chaperonin alpha subunit
E: Chaperonin alpha subunit
F: Chaperonin alpha subunit
G: Chaperonin alpha subunit
H: Chaperonin alpha subunit
I: Chaperonin alpha subunit
J: Chaperonin alpha subunit
K: Chaperonin alpha subunit
L: Chaperonin alpha subunit
M: Chaperonin alpha subunit
N: Chaperonin alpha subunit
O: Chaperonin alpha subunit
P: Chaperonin alpha subunit
Q: Chaperonin alpha subunit
R: Chaperonin alpha subunit


Theoretical massNumber of molelcules
Total (without water)1,084,84718
Polymers1,084,84718
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein
Chaperonin alpha subunit / Thermosome / rATcpn-alpha


Mass: 60269.285 Da / Num. of mol.: 18
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Acidianus tengchongensis (archaea) / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta / References: UniProt: Q877H0

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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: 9-fold symmetric rATcpn-alpha in apo state / Type: COMPLEX
Details: Hexadecamer. This sample has about 90% 8-fold symmetric particles and about 10% 9-fold symmetric particles.
Synonym: Thermosome
Buffer solutionName: Tris-HCl / pH: 7.5 / Details: Tris-HCl
SpecimenConc.: 3 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportDetails: This sample was applied to a 400-mesh GiG grid with holes of 2 um diameter and 2 um spacing.
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: NITROGEN / Humidity: 100 %
Details: Blot for 4 seconds before plunging into liquid nitrogen (FEI Vitrobot Mark IV).

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS / Date: Jul 23, 2010
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 96000 X / Calibrated magnification: 96000 X / Nominal defocus max: 3500 nm / Nominal defocus min: 1500 nm / Cs: 2.7 mm
Specimen holderTemperature: 90 K
Image recordingElectron dose: 20 e/Å2 / Film or detector model: GATAN ULTRASCAN 4000 (4k x 4k) / Details: 4k x 4k
Image scansNum. digital images: 3424
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthRelative weight: 1

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Processing

EM software
IDNameVersionCategory
1UCSF Chimeramodel fitting
2EMAN1.93D reconstruction
3SPIDER3D reconstruction
CTF correctionDetails: The whole micrograph
SymmetryPoint symmetry: C9 (9 fold cyclic)
3D reconstructionResolution: 9.1 Å / Num. of particles: 9596 / Details: Spider, EMAN1.9 / Symmetry type: POINT
Atomic model buildingProtocol: FLEXIBLE FIT / Space: REAL
Details: METHOD--symmetry-restrained MDFF REFINEMENT PROTOCOL--Rigid body and Molecular Dynamics Flexible Fitting
Atomic model buildingPDB-ID: 3KO1

3ko1


Accession code: 3KO1 / Source name: PDB / Type: experimental model
Refinement stepCycle: LAST
ProteinNucleic acidLigandSolventTotal
Num. atoms70866 0 0 0 70866

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