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Open data
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Basic information
Entry | Database: PDB / ID: 6u5z | |||||||||
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Title | Cryo-EM structure of E. coli LonA S679A | |||||||||
![]() | Lon protease | |||||||||
![]() | HYDROLASE / Lon protease / hexamer | |||||||||
Function / homology | ![]() endopeptidase La / ATP-dependent peptidase activity / protein quality control for misfolded or incompletely synthesized proteins / response to X-ray / peptidase activity / cellular response to heat / response to heat / sequence-specific DNA binding / serine-type endopeptidase activity / ATP hydrolysis activity ...endopeptidase La / ATP-dependent peptidase activity / protein quality control for misfolded or incompletely synthesized proteins / response to X-ray / peptidase activity / cellular response to heat / response to heat / sequence-specific DNA binding / serine-type endopeptidase activity / ATP hydrolysis activity / proteolysis / DNA binding / ATP binding / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
![]() | Botos, I. / Lountos, G.T. / Weimin, W. / Wlodawer, A. | |||||||||
Funding support | ![]() ![]()
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![]() | ![]() Title: Cryo-EM structure of substrate-free E. coli Lon protease provides insights into the dynamics of Lon machinery Authors: Botos, I. / Lountos, G.T. / Weimin, W. / Cherry, S. / Ghirlando, R. / Kudzhaev, A.M. / Rotanova, T.V. / de Val, N. / Tropea, J. / Gustchina, A. / Wlodawer, A. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 540.4 KB | Display | ![]() |
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PDB format | ![]() | 455.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 867.5 KB | Display | ![]() |
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Full document | ![]() | 892.4 KB | Display | |
Data in XML | ![]() | 81.8 KB | Display | |
Data in CIF | ![]() | 121.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 20659MC M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | Mass: 87546.266 Da / Num. of mol.: 6 / Mutation: S679A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: lon, ACN002_0456, CV83915_01127, ECs0493, EL75_3311, EL80_3360 Production host: ![]() ![]() References: UniProt: C3TLS2, UniProt: P0A9M0*PLUS, endopeptidase La |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: ATP-dependent protease La / Type: COMPLEX / Details: S679A mutant / Entity ID: all / Source: RECOMBINANT |
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Molecular weight | Value: 0.087 MDa / Experimental value: YES |
Source (natural) | Organism: ![]() ![]() |
Source (recombinant) | Organism: ![]() ![]() |
Buffer solution | pH: 7.2 |
Specimen | Conc.: 1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Grid type: Quantifoil R1.2/1.3 |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 50 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
Software | Name: PHENIX / Version: 1.15.2_3472: / Classification: refinement | ||||||||||||||||||||||||||||||||||||
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EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||
Particle selection | Num. of particles selected: 889189 | ||||||||||||||||||||||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 274765 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||
Atomic model building | Space: REAL | ||||||||||||||||||||||||||||||||||||
Refine LS restraints |
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