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- EMDB-20210: Synthetic beta-carboxysome shell (T=4) -

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Basic information

Entry
Database: EMDB / ID: EMD-20210
TitleSynthetic beta-carboxysome shell (T=4)
Map datasharpened and cropped map used for figures.
Sample
  • Complex: Synthetic beta-carboxysome shell (prolate symmetry expansion focused refinement)
Biological speciesHalothece sp. PCC 7418 (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.7 Å
AuthorsSutter M / Laughlin TG / Sloan NB / Serwas D / Davies KM / Kerfeld CA
Funding support United States, 3 items
OrganizationGrant numberCountry
Department of Energy (United States)DE-FG02-91ER20021 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases5 R01 AI114975-05 United States
Department of Energy (United States)DE-AC02-O5CH11231 United States
CitationJournal: Plant Physiol / Year: 2019
Title: Structure of a Synthetic -Carboxysome Shell.
Authors: Markus Sutter / Thomas G Laughlin / Nancy B Sloan / Daniel Serwas / Karen M Davies / Cheryl A Kerfeld /
Abstract: Carboxysomes are capsid-like, CO-fixing organelles that are present in all cyanobacteria and some chemoautotrophs and that substantially contribute to global primary production. They are composed of ...Carboxysomes are capsid-like, CO-fixing organelles that are present in all cyanobacteria and some chemoautotrophs and that substantially contribute to global primary production. They are composed of a selectively permeable protein shell that encapsulates Rubisco, the principal CO-fixing enzyme, and carbonic anhydrase. As the centerpiece of the carbon-concentrating mechanism, by packaging enzymes that collectively enhance catalysis, the carboxysome shell enables the generation of a locally elevated concentration of substrate CO and the prevention of CO escape. A functional carboxysome consisting of an intact shell and cargo is essential for cyanobacterial growth under ambient CO concentrations. Using cryo-electron microscopy, we have determined the structure of a recombinantly produced simplified β-carboxysome shell. The structure reveals the sidedness and the specific interactions between the carboxysome shell proteins. The model provides insight into the structural basis of selective permeability of the carboxysome shell and can be used to design modifications to investigate the mechanisms of cargo encapsulation and other physiochemical properties such as permeability. Notably, the permeability properties are of great interest for modeling and evaluating this carbon-concentrating mechanism in metabolic engineering. Moreover, we find striking similarity between the carboxysome shell and the structurally characterized, evolutionarily distant metabolosome shell, implying universal architectural principles for bacterial microcompartment shells.
History
DepositionMay 6, 2019-
Header (metadata) releaseJul 24, 2019-
Map releaseSep 25, 2019-
UpdateSep 25, 2019-
Current statusSep 25, 2019Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 3.5
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 3.5
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_20210.png

Downloads & links

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Map

FileDownload / File: emd_20210.map.gz / Format: CCP4 / Size: 27.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationsharpened and cropped map used for figures.
Voxel sizeX=Y=Z: 0.8908 Å
Density
Contour LevelBy AUTHOR: 3.5 / Movie #1: 3.5
Minimum - Maximum-7.5397353 - 21.883955
Average (Standard dev.)0.000000000004526 (±1.0)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderZYX
Origin8552154
Dimensions170217198
Spacing198170217
CellA: 176.3784 Å / B: 151.436 Å / C: 193.3036 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z0.890797979797980.89080.89080184331797
M x/y/z198170217
origin x/y/z0.0000.0000.000
length x/y/z176.378151.436193.304
α/β/γ90.00090.00090.000
start NX/NY/NZ1548552
NX/NY/NZ198170217
MAP C/R/S321
start NC/NR/NS5285154
NC/NR/NS217170198
D min/max/mean-7.54021.8840.000

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Supplemental data

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Mask #1

Fileemd_20210_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: shell (T=4)

Fileemd_20210_half_map_1.map
Annotationshell (T=4)
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: shell (T=4)

Fileemd_20210_half_map_2.map
Annotationshell (T=4)
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Synthetic beta-carboxysome shell (prolate symmetry expansion focu...

EntireName: Synthetic beta-carboxysome shell (prolate symmetry expansion focused refinement)
Components
  • Complex: Synthetic beta-carboxysome shell (prolate symmetry expansion focused refinement)

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Supramolecule #1: Synthetic beta-carboxysome shell (prolate symmetry expansion focu...

SupramoleculeName: Synthetic beta-carboxysome shell (prolate symmetry expansion focused refinement)
type: complex / ID: 1 / Parent: 0 / Details: bacterial microcompartment
Source (natural)Organism: Halothece sp. PCC 7418 (bacteria)
Recombinant expressionOrganism: Escherichia coli (E. coli)

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.6 mg/mL
BufferpH: 8
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV / Details: blot for 6 seconds before plunging.

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsCalibrated magnification: 56000 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.5 µm
Specialist opticsEnergy filter - Name: GIF Quantum LS / Energy filter - Slit width: 25 eV
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Digitization - Frames/image: 1-25 / Number grids imaged: 1 / Number real images: 1343 / Average exposure time: 6.0 sec. / Average electron dose: 50.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 47121
CTF correctionSoftware: (Name: Gctf (ver. 1.06), RELION (ver. 3.0.b2))
Startup modelType of model: INSILICO MODEL / In silico model: ab initio model generated with cryosparc
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 2)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0b2)
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Algorithm: BACK PROJECTION / Resolution.type: BY AUTHOR / Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0.b2)
Details: number of particles corresponds to the number after symmetry expansion
Number images used: 16942
FSC plot (resolution estimation)

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