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- EMDB-11271: E2 core of the fungal Pyruvate dehydrogenase complex with asymmet... -

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Basic information

Entry
Database: EMDB / ID: EMD-11271
TitleE2 core of the fungal Pyruvate dehydrogenase complex with asymmetric interior PX261 component
Map dataFungal PDC (N. crassa). Recombinant preparation-tE2/PX261. Enforced symmetry: I2. Periphery (PX only) is absent. Core is structured. Interior is oversymm.
Sample
  • Complex: E2 core of the fungal Pyruvate dehydrogenase complex with asymmetric inetrior PX261 component
Biological speciesNeurospora crassa (fungus)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.1 Å
AuthorsForsberg BO / Lindahl E / Aibara S / Howard RJ / Mortezaei N
Funding support Sweden, European Union, 5 items
OrganizationGrant numberCountry
Swedish Research Council2015-04107 Sweden
European Research Council (ERC)ERC-2018-StG-805230European Union
Swedish Research Council2017-04641 Sweden
Knut and Alice Wallenberg Foundation2018.0080 Sweden
European Research Council (ERC)bioexcel-823830European Union
CitationJournal: Nat Commun / Year: 2020
Title: Arrangement and symmetry of the fungal E3BP-containing core of the pyruvate dehydrogenase complex.
Authors: B O Forsberg / S Aibara / R J Howard / N Mortezaei / E Lindahl /
Abstract: The pyruvate dehydrogenase complex (PDC) is a multienzyme complex central to aerobic respiration, connecting glycolysis to mitochondrial oxidation of pyruvate. Similar to the E3-binding protein (E3BP) ...The pyruvate dehydrogenase complex (PDC) is a multienzyme complex central to aerobic respiration, connecting glycolysis to mitochondrial oxidation of pyruvate. Similar to the E3-binding protein (E3BP) of mammalian PDC, PX selectively recruits E3 to the fungal PDC, but its divergent sequence suggests a distinct structural mechanism. Here, we report reconstructions of PDC from the filamentous fungus Neurospora crassa by cryo-electron microscopy, where we find protein X (PX) interior to the PDC core as opposed to substituting E2 core subunits as in mammals. Steric occlusion limits PX binding, resulting in predominantly tetrahedral symmetry, explaining previous observations in Saccharomyces cerevisiae. The PX-binding site is conserved in (and specific to) fungi, and complements possible C-terminal binding motifs in PX that are absent in mammalian E3BP. Consideration of multiple symmetries thus reveals a differential structural basis for E3BP-like function in fungal PDC.
History
DepositionJun 30, 2020-
Header (metadata) releaseSep 23, 2020-
Map releaseSep 23, 2020-
UpdateDec 16, 2020-
Current statusDec 16, 2020Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.016
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.016
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_11271.png

Downloads & links

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Map

FileDownload / File: emd_11271.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationFungal PDC (N. crassa). Recombinant preparation-tE2/PX261. Enforced symmetry: I2. Periphery (PX only) is absent. Core is structured. Interior is oversymm.
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.86 Å/pix.
x 384 pix.
= 330.24 Å		0.86 Å/pix.
x 384 pix.
= 330.24 Å		0.86 Å/pix.
x 384 pix.
= 330.24 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.86 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.016 / Movie #1: 0.016
Minimum - Maximum-0.057006128 - 0.10598068
Average (Standard dev.)0.00041068433 (±0.0045012645)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 330.24 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z0.860.860.86
M x/y/z384384384
origin x/y/z0.0000.0000.000
length x/y/z330.240330.240330.240
α/β/γ90.00090.00090.000
start NX/NY/NZ1081340
NX/NY/NZ13584349
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS384384384
D min/max/mean-0.0570.1060.000

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Supplemental data

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Additional map: Fungal PDC (N. crassa). Recombinant preparation-tE2/PX261. Enforced symmetry:...

Fileemd_11271_additional.map
AnnotationFungal PDC (N. crassa). Recombinant preparation-tE2/PX261. Enforced symmetry: I2. Periphery (PX only) is absent. Core is structured. Interior is oversymm. Unmasked
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: Fungal PDC (N. crassa). Recombinant preparation-tE2/PX261. Enforced symmetry:...

Fileemd_11271_additional_1.map
AnnotationFungal PDC (N. crassa). Recombinant preparation-tE2/PX261. Enforced symmetry: I2. Periphery (PX only) is absent. Core is structured. Interior is oversymm. Unmasked
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : E2 core of the fungal Pyruvate dehydrogenase complex with asymmet...

EntireName: E2 core of the fungal Pyruvate dehydrogenase complex with asymmetric inetrior PX261 component
Components
  • Complex: E2 core of the fungal Pyruvate dehydrogenase complex with asymmetric inetrior PX261 component

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Supramolecule #1: E2 core of the fungal Pyruvate dehydrogenase complex with asymmet...

SupramoleculeName: E2 core of the fungal Pyruvate dehydrogenase complex with asymmetric inetrior PX261 component
type: complex / ID: 1 / Parent: 0
Source (natural)Organism: Neurospora crassa (fungus)
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

Concentration3 mg/mL
BufferpH: 7.5
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 31.4 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Point group: I (icosahedral) / Resolution.type: BY AUTHOR / Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 306327
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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