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- EMDB-29093: Focused refinement of V. radiata respiratory supercomplex I+III2 ... -

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Entry
Database: EMDB / ID: EMD-29093
TitleFocused refinement of V. radiata respiratory supercomplex I+III2 around complex III2 proximal MPP domain
Map dataFocused refinement of bridged SC I III2 class 1 around CIII2 proximal MPP domain
Sample
  • Complex: Vigna radiata supercomplex I+III2 (full bridge)
Biological speciesVigna radiata (mung bean)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsMaldonado M / Letts JA
Funding support United States, 1 items
OrganizationGrant numberCountry
Department of Energy (DOE, United States)DE-SC0022293 United States
CitationJournal: Nat Plants / Year: 2023
Title: Plant-specific features of respiratory supercomplex I + III from Vigna radiata.
Authors: M Maldonado / Z Fan / K M Abe / J A Letts /
Abstract: The last steps of cellular respiration-an essential metabolic process in plants-are carried out by mitochondrial oxidative phosphorylation. This process involves a chain of multi-subunit membrane ...The last steps of cellular respiration-an essential metabolic process in plants-are carried out by mitochondrial oxidative phosphorylation. This process involves a chain of multi-subunit membrane protein complexes (complexes I-V) that form higher-order assemblies called supercomplexes. Although supercomplexes are the most physiologically relevant form of the oxidative phosphorylation complexes, their functions and structures remain mostly unknown. Here we present the cryogenic electron microscopy structure of the supercomplex I + III from Vigna radiata (mung bean). The structure contains the full subunit complement of complex I, including a newly assigned, plant-specific subunit. It also shows differences in the mitochondrial processing peptidase domain of complex III relative to a previously determined supercomplex with complex IV. The supercomplex interface, while reminiscent of that in other organisms, is plant specific, with a major interface involving complex III's mitochondrial processing peptidase domain and no participation of complex I's bridge domain. The complex I structure suggests that the bridge domain sets the angle between the enzyme's two arms, limiting large-scale conformational changes. Moreover, complex I's catalytic loops and its response in active-to-deactive assays suggest that, in V. radiata, the resting complex adopts a non-canonical state and can sample deactive- or open-like conformations even in the presence of substrate. This study widens our understanding of the possible conformations and behaviour of complex I and supercomplex I + III. Further studies of complex I and its supercomplexes in diverse organisms are needed to determine the universal and clade-specific mechanisms of respiration.
History
DepositionDec 14, 2022-
Header (metadata) releaseJan 11, 2023-
Map releaseJan 11, 2023-
UpdateFeb 8, 2023-
Current statusFeb 8, 2023Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_29093.png

Downloads & links

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Map

FileDownload / File: emd_29093.map.gz / Format: CCP4 / Size: 824 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationFocused refinement of bridged SC I III2 class 1 around CIII2 proximal MPP domain
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.88 Å/pix.
x 600 pix.
= 528. Å		0.88 Å/pix.
x 600 pix.
= 528. Å		0.88 Å/pix.
x 600 pix.
= 528. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.88 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.15
Minimum - Maximum-1.7591499 - 2.3787875
Average (Standard dev.)0.0002088869 (±0.023120133)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions600600600
Spacing600600600
CellA=B=C: 528.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_29093_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Focused refinement of bridged SC I III2 class...

Fileemd_29093_half_map_1.map
AnnotationFocused refinement of bridged SC I III2 class 1 around CIII2 proximal MPP domain half map A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Focused refinement of bridged SC I III2 class...

Fileemd_29093_half_map_2.map
AnnotationFocused refinement of bridged SC I III2 class 1 around CIII2 proximal MPP domain half map B
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Vigna radiata supercomplex I+III2 (full bridge)

EntireName: Vigna radiata supercomplex I+III2 (full bridge)
Components
  • Complex: Vigna radiata supercomplex I+III2 (full bridge)

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Supramolecule #1: Vigna radiata supercomplex I+III2 (full bridge)

SupramoleculeName: Vigna radiata supercomplex I+III2 (full bridge) / type: complex / ID: 1 / Chimera: Yes / Parent: 0 / Macromolecule list: #1-#40, #42-#59
Details: Higher-order assembly between respiratory complex I and complex III2
Source (natural)Organism: Vigna radiata (mung bean)

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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

Concentration1.55 mg/mL
BufferpH: 7.7
Details: 0.2% digitonin, 30 mM HEPES pH 7.7, 150 mM potassium acetate, 1 mM EDTA, 0.002% PMSF
VitrificationCryogen name: ETHANE / Chamber humidity: 90 % / Instrument: LEICA EM GP / Details: 4 ul, 20 seconds pre-blot, blot 4 seconds.
DetailsDigitonin-extracted, amphipol (A8-35)stabilized

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Electron microscopy

MicroscopeTFS GLACIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 2 / Number real images: 25712 / Average exposure time: 3.0 sec. / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: OTHER / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.5 µm
Sample stageCooling holder cryogen: NITROGEN

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Image processing

Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 123461
Initial angle assignmentType: NOT APPLICABLE
Final angle assignmentType: NOT APPLICABLE
FSC plot (resolution estimation)

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Atomic model buiding 1

RefinementSpace: REAL / Protocol: RIGID BODY FIT

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