Atomic Model of Mm-cpn in the Closed State
by single particle reconstruction, at 4.3 A resolution

#1: Depositted structure unit, Made by Jmol
#2: Superimposing with EM 3D map: EMDB-5137, Made by UCSF CHIMERA
Entry | |
| Summary | |
| Database / ID | PORTEIN DATA BANK (PDB) / 3los |
|---|---|
| Title | Atomic Model of Mm-cpn in the Closed State |
| Descriptor | Chaperonin |
| Keywords | CHAPERONE, Group II chaperonin, Protein Folding, Mm-cpn, Single Particle Reconstruction, Methanococcus maripaludis, Chaperone, ATP-binding, Nucleotide-binding |
| Authors | Zhang, J., Baker, M.L., Schroeder, G., Douglas, N.R., Reissmann, S., Jakana, J., Dougherty, M., Fu, C.J., Levitt, M., Ludtke, S.J., Frydman, J., Chiu, W. |
| Date | Deposition: 2010-02-04, Release: 2010-03-16 |
| PDBj Mine pages | Summary, Structural Details, Experimental Details, Functional Details |
| Other databases | RCSB-PDB, PDBe, CATH, CE, FSSP, SCOP, VAST |
| Structure Visualization | |
| Movies | Movie Page#1: Depositted structure unit, Made by Jmol #2: Superimposing with EM 3D map: EMDB-5137, Made by UCSF CHIMERA |
| Structure viewers | Yorodumi, jV4, Jmol, Biological unit (Images, jV) |
| Related Structure Data | |
| Related Entries |
Cite: data citing same article Fit: target map of fitting |
| Similar strucutres (beta) |
List of similar structure data about Omokage system |
Article | |
| Citation - primary | |
| Article | Nature, Vol. 463, Issue 7279, Page 379-83, Year 2010 |
|---|---|
| Title | Mechanism of folding chamber closure in a group II chaperonin. |
| Authors | Junjie Zhang, Matthew L Baker, Gunnar F Schröder, Nicholai R Douglas, Stefanie Reissmann, Joanita Jakana, Matthew Dougherty, Caroline J Fu, Michael Levitt, Steven J Ludtke, Judith Frydman, Wah Chiu Graduate Program in Structural and Computational Biology and Molecular Biophysics, Baylor College of Medicine, Houston, Texas 77030, USA. |
| Keywords | Adenosine Triphosphate (chemistry, 56-65-5), Allosteric Regulation, Binding Sites, Cryoelectron Microscopy, Group II Chaperonins (chemistry, 3.6.1.-), Hydrolysis (drug effects), Methanococcus (chemistry), Models, Molecular, Protein Binding, Protein Conformation (drug effects), Protein Folding, Protein Subunits (chemistry), Structure-Activity Relationship |
| Links | DOI: 10.1038/nature08701, PubMed: 20090755, PMC: PMC2834796 |
Components | |
| ID 1 : Chaperonin GroEL (Thermosome, HSP60 family) | |
| Image | ![]() ![]() |
|---|---|
| Description | Chaperonin |
| Type | polymer |
| Formula weight | 58290.793 Da |
| Number of molecules | 16 |
| Source | Method: Isolated from a genetically manipulated source Gene: hsp60, MMP1515, ID:39152, Methanococcus maripaludisHost: ID:562, Escherichia coli |
| Links | UniProt: Q877G8, Sequence view |
Sample | |
| Assembly | |
| Aggregation state | PARTICLE |
|---|---|
| Composition | 16-mer |
| Experimental Mass | 0.96 |
| Theoretical Mass | 0.96 |
| Name | Mm-cpn with 1mM ATP/AlFx |
| Num components | 1 |
| Entity assembly | |
| Name | Methanococcus maripaludis chaperonin |
| Type | PROTEIN |
| Buffer | |
| Name | ATPase buffer |
| Experiment | |
| Reconstruction method | SINGLE PARTICLE |
| Specimen type | VITREOUS ICE (CRYO EM) |
| Sample preparation | |
| pH | 7.5 |
| Vitrification | |
| Cryogen name | ETHANE |
| Humidity | 100 |
| Instrument | Vitrobot |
| Method | 1 blot 3 seconds |
Electron Microscopy | |
| Imaging | |
| Microscope | model: JEM3200FSC |
|---|---|
| Electron gun | |
| Electron source | FIELD EMISSION GUN |
| Accelerating voltage | 300 kV |
| Electron dose | 20 e/A**2 |
| Illumination mode | FLOOD BEAM |
| Lens | |
| Mode | BRIGHT FIELD |
| Magnification | calibrated: 112000 X, nominal: 80000 X |
| Cs | nominal: 4.1 mm |
| Astigmatism | objective lens astigmatism was corrected at 100,000 times magnification |
| Detector distance | 0.0 |
| Nominal defocus | max: 3000 nm, min: 1000 nm |
| Energy filter | in column omega filter |
| Energy window | 0-10 eV |
| Specimen holder | |
| Specimen holder | model: JEM3200FSC CRYOHOLDER, type: side-entry |
| Tilt angle | min: 0.0 degrees, max: 0.0 degrees |
| Temperature | 100 Kelvin |
| Detector | |
| Type | Gatan 4kX4k CCD Camera |
Processing | |
| Single particle entity | |
| Symmetry type | DIHEDRAL |
|---|---|
| 3D reconstruction | |
| CTF correction method | Each micrograph |
| Details | THE SINGLE SUBUNIT MODEL OF MM-CPN WAS MANUALLY BUILT IN THE CRYO-EM DENSITY USING COOT. THE ENTIRE 16-SUBUNIT COMPLEX WAS GENERATED BASED ON THE D8 SYMMETRY. |
| Method | Projection-match |
| Resolution | 4.3 A |
| Resolution method | FSC at 0.5 cut-off |
| Software | EMAN |
| 3D fitting | |
| Details | THE SINGLE SUBUNIT MODEL OF MM-CPN WAS MANUALLY BUILT IN THE CRYO-EM DENSITY USING COOT. THE ENTIRE 16-SUBUNIT COMPLEX WAS GENERATED BASED ON THE D8 SYMMETRY. |
| Refine hist | |
| Total atoms | 63712 |
| Protein atoms | 63712 |
Download | |||
| PDB format | |||
| All | pdb3los.ent.gz pdb3los.ent (uncompressed file) | ||
|---|---|---|---|
| Header only | pdb3los.ent.gz | ||
| mmCIF format | |||
| mmCIF | 3los.cif.gz | ||
| XML format | |||
| All | 3los.xml.gz | ||
| No-atom | 3los-noatom.xml.gz | ||
| Ext-atom | 3los-extatom.xml.gz | ||
| Movie files | |||
| movie #1 |
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| movie #2 |
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