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- PDB-6mzy: Cryo-EM structure of the HO BMC shell: Icosahedral reconstruction... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6mzy | |||||||||
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Title | Cryo-EM structure of the HO BMC shell: Icosahedral reconstruction of the compacted subpopulation | |||||||||
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![]() | STRUCTURAL PROTEIN / microcompartment / shell / compartmentalization / BMC fold | |||||||||
Function / homology | ![]() | |||||||||
Biological species | ![]() | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||
![]() | Greber, B.J. / Sutter, M. / Kerfeld, C.A. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: The Plasticity of Molecular Interactions Governs Bacterial Microcompartment Shell Assembly. Authors: Basil J Greber / Markus Sutter / Cheryl A Kerfeld / ![]() Abstract: Bacterial microcompartments (BMCs) are composed of an enzymatic core encapsulated by a selectively permeable protein shell that enhances catalytic efficiency. Many pathogenic bacteria derive ...Bacterial microcompartments (BMCs) are composed of an enzymatic core encapsulated by a selectively permeable protein shell that enhances catalytic efficiency. Many pathogenic bacteria derive competitive advantages from their BMC-based catabolism, implicating BMCs as drug targets. BMC shells are of interest for bioengineering due to their diverse and selective permeability properties and because they self-assemble. A complete understanding of shell composition and organization is a prerequisite for biotechnological applications. Here, we report the cryoelectron microscopy structure of a BMC shell at 3.0-Å resolution, using an image-processing strategy that allowed us to determine the previously uncharacterized structural details of the interactions formed by the BMC-T and BMC-T shell subunits in the context of the assembled shell. We found unexpected structural plasticity among these interactions, resulting in distinct shell populations assembled from varying numbers of the BMC-T and BMC-T subunits. We discuss the implications of these findings on shell assembly and function. | |||||||||
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 | ![]() | 170.3 KB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 1.3 MB | Display | ![]() |
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Full document | ![]() | 1.3 MB | Display | |
Data in XML | ![]() | 43.7 KB | Display | |
Data in CIF | ![]() | 63.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9310MC ![]() 9296C ![]() 9307C ![]() 9308C ![]() 9309C ![]() 9311C ![]() 9312C ![]() 9313C ![]() 9314C ![]() 9315C ![]() 6mzuC ![]() 6mzvC ![]() 6mzxC ![]() 6n06C ![]() 6n07C ![]() 6n09C ![]() 6n0fC ![]() 6n0gC 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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3 | ![]()
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Symmetry | Point symmetry: (Schoenflies symbol: I (icosahedral)) |
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Components
#1: Protein | Mass: 9866.319 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: DSM 14365 / JCM 11303 / SMP-2 / Gene: Hoch_5814 / Production host: ![]() ![]() | ||
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#2: Protein | Mass: 10126.718 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: DSM 14365 / JCM 11303 / SMP-2 / Gene: Hoch_5815 / Production host: ![]() ![]() #3: Protein | Mass: 22904.137 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: DSM 14365 / JCM 11303 / SMP-2 / Gene: Hoch_5816 / Production host: ![]() ![]() |
-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: Bacterial microcompartment shell from Haliangium ochraceum Type: ORGANELLE OR CELLULAR COMPONENT / Entity ID: all / Source: RECOMBINANT | ||||||||||||||||||||
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Molecular weight | Value: 6.5 MDa / Experimental value: NO | ||||||||||||||||||||
Source (natural) | Organism: ![]() | ||||||||||||||||||||
Source (recombinant) | Organism: ![]() ![]() | ||||||||||||||||||||
Buffer solution | pH: 7.4 | ||||||||||||||||||||
Buffer component |
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Specimen | Conc.: 3 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||
Specimen support | Details: unspecified | ||||||||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K Details: 5-7 sec incubation of the sample on the grid before blotting and plunging |
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Electron microscopy imaging
Microscopy | Model: FEI TITAN |
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Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Calibrated magnification: 48543 X / Calibrated defocus min: 1000 nm / Calibrated defocus max: 3500 nm / Cs: 2.7 mm / C2 aperture diameter: 50 µm / Alignment procedure: COMA FREE |
Specimen holder | Cryogen: NITROGEN Specimen holder model: GATAN 626 SINGLE TILT LIQUID NITROGEN CRYO TRANSFER HOLDER |
Image recording | Average exposure time: 4.5 sec. / Electron dose: 25 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 928 Details: 928 images retained after inspection for image quality. Movie frames were aligned and dose weighed using Motioncor2. |
Image scans | Sampling size: 5 µm / Width: 3838 / Height: 3710 / Movie frames/image: 30 / Used frames/image: 1-30 |
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Processing
EM software |
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CTF correction | Details: Initial CTF fitting using CTFFIND4, CTF correction applied within RELION. Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||
Particle selection | Num. of particles selected: 31800 Details: 1000 particles were picked manually to generate reference templates for subsequent auto-picking in RELION 1.4. | ||||||||||||||||||||||||||||||||||||||||
Symmetry | Point symmetry: I (icosahedral) | ||||||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 2276 / Algorithm: FOURIER SPACE Details: Frequency-limited refinement in FREALIGN. To avoid overfitting, resolutions higher than 3.6 Angstroms were excluded from the refinement. Icosahedral symmetry was imposed throughout the refinement procedure. Num. of class averages: 1 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||
Atomic model building | Protocol: OTHER / Space: REAL | ||||||||||||||||||||||||||||||||||||||||
Atomic model building | PDB-ID: 5V74 Accession code: 5V74 / Source name: PDB / Type: experimental model |