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- EMDB-4584: Structure and assembly of the mitochondrial membrane remodelling ... -

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Basic information

Entry
Database: EMDB / ID: EMD-4584
TitleStructure and assembly of the mitochondrial membrane remodelling GTPase Mgm1
Map dataNone
Sample
  • Complex: Mgm1
    • Protein or peptide: Mgm1
Function / homology
Function and homology information


GTPase-dependent fusogenic activity / membrane bending activity / dynamin GTPase / mitochondrial intermembrane space / mitochondrial inner membrane / GTPase activity / lipid binding / GTP binding / metal ion binding
Similarity search - Function
Dynamin, GTPase region, conserved site / Dynamin-type guanine nucleotide-binding (G) domain signature. / Dynamin stalk domain / Dynamin central region / GTPase effector domain / GED domain profile. / Dynamin, GTPase domain / Dynamin, GTPase / Dynamin / Dynamin-type guanine nucleotide-binding (G) domain ...Dynamin, GTPase region, conserved site / Dynamin-type guanine nucleotide-binding (G) domain signature. / Dynamin stalk domain / Dynamin central region / GTPase effector domain / GED domain profile. / Dynamin, GTPase domain / Dynamin, GTPase / Dynamin / Dynamin-type guanine nucleotide-binding (G) domain / Dynamin-type guanine nucleotide-binding (G) domain profile. / Dynamin, N-terminal / Dynamin family / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Dynamin-like GTPase MGM1, mitochondrial
Similarity search - Component
Biological speciesChaetomium thermophilum var. thermophilum DSM 1495 (fungus) / Chaetomium thermophilum (fungus)
Methodsubtomogram averaging / cryo EM / Resolution: 20.4 Å
AuthorsFaelber K / Dietrich L / Noel J / Wollweber F / Pfitzner A / Muehleip A / Sanchez R / Kudryashev M / Chiaruttin N / Lilie H ...Faelber K / Dietrich L / Noel J / Wollweber F / Pfitzner A / Muehleip A / Sanchez R / Kudryashev M / Chiaruttin N / Lilie H / Schleger J / Rosenbaum E / Hessenberger M / Matthaeus C / Noe F / Roux A / van der Laan M / Kuehlbrandt W / Daumke O
Funding support Germany, 1 items
OrganizationGrant numberCountry
Max Planck Society Germany
CitationJournal: Nature / Year: 2019
Title: Structure and assembly of the mitochondrial membrane remodelling GTPase Mgm1.
Authors: Katja Faelber / Lea Dietrich / Jeffrey K Noel / Florian Wollweber / Anna-Katharina Pfitzner / Alexander Mühleip / Ricardo Sánchez / Misha Kudryashev / Nicolas Chiaruttini / Hauke Lilie / ...Authors: Katja Faelber / Lea Dietrich / Jeffrey K Noel / Florian Wollweber / Anna-Katharina Pfitzner / Alexander Mühleip / Ricardo Sánchez / Misha Kudryashev / Nicolas Chiaruttini / Hauke Lilie / Jeanette Schlegel / Eva Rosenbaum / Manuel Hessenberger / Claudia Matthaeus / Séverine Kunz / Alexander von der Malsburg / Frank Noé / Aurélien Roux / Martin van der Laan / Werner Kühlbrandt / Oliver Daumke /
Abstract: Balanced fusion and fission are key for the proper function and physiology of mitochondria. Remodelling of the mitochondrial inner membrane is mediated by the dynamin-like protein mitochondrial ...Balanced fusion and fission are key for the proper function and physiology of mitochondria. Remodelling of the mitochondrial inner membrane is mediated by the dynamin-like protein mitochondrial genome maintenance 1 (Mgm1) in fungi or the related protein optic atrophy 1 (OPA1) in animals. Mgm1 is required for the preservation of mitochondrial DNA in yeast, whereas mutations in the OPA1 gene in humans are a common cause of autosomal dominant optic atrophy-a genetic disorder that affects the optic nerve. Mgm1 and OPA1 are present in mitochondria as a membrane-integral long form and a short form that is soluble in the intermembrane space. Yeast strains that express temperature-sensitive mutants of Mgm1 or mammalian cells that lack OPA1 display fragmented mitochondria, which suggests that Mgm1 and OPA1 have an important role in inner-membrane fusion. Consistently, only the mitochondrial outer membrane-not the inner membrane-fuses in the absence of functional Mgm1. Mgm1 and OPA1 have also been shown to maintain proper cristae architecture; for example, OPA1 prevents the release of pro-apoptotic factors by tightening crista junctions. Finally, the short form of OPA1 localizes to mitochondrial constriction sites, where it presumably promotes mitochondrial fission. How Mgm1 and OPA1 perform their diverse functions in membrane fusion, scission and cristae organization is at present unknown. Here we present crystal and electron cryo-tomography structures of Mgm1 from Chaetomium thermophilum. Mgm1 consists of a GTPase (G) domain, a bundle signalling element domain, a stalk, and a paddle domain that contains a membrane-binding site. Biochemical and cell-based experiments demonstrate that the Mgm1 stalk mediates the assembly of bent tetramers into helical filaments. Electron cryo-tomography studies of Mgm1-decorated lipid tubes and fluorescence microscopy experiments on reconstituted membrane tubes indicate how the tetramers assemble on positively or negatively curved membranes. Our findings convey how Mgm1 and OPA1 filaments dynamically remodel the mitochondrial inner membrane.
History
DepositionFeb 1, 2019-
Header (metadata) releaseFeb 20, 2019-
Map releaseAug 14, 2019-
UpdateNov 25, 2020-
Current statusNov 25, 2020Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 1
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 1
  • Imaged by UCSF Chimera
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Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_4584.png

Downloads & links

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Map

FileDownload / File: emd_4584.map.gz / Format: CCP4 / Size: 83.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationNone
Projections & slices

Image control

Size
Brightness
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Others
AxesZ (Sec.)Y (Row.)X (Col.)
2.7 Å/pix.
x 280 pix.
= 756. Å		2.7 Å/pix.
x 280 pix.
= 756. Å		2.7 Å/pix.
x 280 pix.
= 756. Å

Surface

Projections

Slices (1/3)

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Images are generated by Spider.

Voxel sizeX=Y=Z: 2.7 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 1 / Movie #1: 1
Minimum - Maximum-1.7201262 - 4.816501
Average (Standard dev.)0.1455895 (±0.5640174)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions280280280
Spacing280280280
CellA=B=C: 756.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z2.72.72.7
M x/y/z280280280
origin x/y/z0.0000.0000.000
length x/y/z756.000756.000756.000
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ320320320
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS280280280
D min/max/mean-1.7204.8170.146

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Supplemental data

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Mask #1

Fileemd_4584_msk_1.map
Projections & Slices
AxesZYX

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Histogram

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Half map: Unfiltered non-masked half-map #1

Fileemd_4584_half_map_1.map
AnnotationUnfiltered non-masked half-map #1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Unfiltered non-masked half-map #2

Fileemd_4584_half_map_2.map
AnnotationUnfiltered non-masked half-map #2
Projections & Slices
AxesZYX

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Histogram

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Sample components

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Entire : Mgm1

EntireName: Mgm1
Components
  • Complex: Mgm1
    • Protein or peptide: Mgm1

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Supramolecule #1: Mgm1

SupramoleculeName: Mgm1 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all / Details: short isoform with C- and N-terminal truncations
Source (natural)Organism: Chaetomium thermophilum var. thermophilum DSM 1495 (fungus)
Recombinant expressionOrganism: Escherichia coli (E. coli)

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Macromolecule #1: Mgm1

MacromoleculeName: Mgm1 / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO / EC number: dynamin GTPase
Source (natural)Organism: Chaetomium thermophilum (fungus)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: Chain A RD DNMMFITKKM IEIRNLLQKV GQGSTVTLPS IVVIGSQSSG KSSVLEAIVG HEFLPKGSNM ITRRPIELTL VNDPEAKVDY GEFPDLGLAR VTDFSLIQKT LTELNQSVTD DPIRLTIHSP NIPDLSLIDL PGYILKRKIT ELCDKYIRGP NIILAISAAD ...String:
Chain A RD DNMMFITKKM IEIRNLLQKV GQGSTVTLPS IVVIGSQSSG KSSVLEAIVG HEFLPKGSNM ITRRPIELTL VNDPEAKVDY GEFPDLGLAR VTDFSLIQKT LTELNQSVTD DPIRLTIHSP NIPDLSLIDL PGYILKRKIT ELCDKYIRGP NIILAISAAD TDLANSTALQ ASRRVDPRGE RTIGVITKMD LVEPEKGAAI LSDRQYPLKL GYVGVISKGN LLASINRNEK NYFGSHPTEF GPDSGVSTGV MTLRKKLLQV LEQQMSSKLN ETTEAIQREL EETTYQFKVQ YNEQPMSAES YLAASLDDFK HQFHEFASSF GRPQLQTLLK DALDQKVLDQ LAARYWNRPI EDLSPAPREP DNIIDLPKAD PDSPYWHRQL DTACSGLTRL GVGRLAATVA ASAIQQHVEK LLDKSSFAKH PSARKVISDA AATVLADRSY ATSDGIEISL KPYKFDPDIQ PNEWAQGREH VVGVLQAELE QCQAAMKALE NSVGGRKKLK EVMSFVDKAR KGEIIVEGDH PSGAGGFSAA LLARGREAVF LRDRADILSL RIQAAKSRQC KTLTNKYYCP EVFLDAVATK LAQTAVLFLN VEMLNDFYVR FPREVEAKLH EHMHAGGGLE KFAREDPKVR RHLDLIRRKE LLETVLGKIE ELHRISSG C hain B DDN MMFITKKMIE IRNLLQKVGQ GSTVTLPSIV VIGSQSSGKS SVLEAIVGHE FLPKGSNMIT RRPIELTLVN DPEAKVDYGE FPDLGLARVT DFSLIQKTLT ELNQSVTDDP IRLTIHSPNI PDLSLIDLPG YILKRKITEL CDKYIRGPNI ILAISAADTD LANSTALQAS RRVDPRGERT IGVITKMDLV EPEKGAAILS DRQYPLKLGY VGVISKGNLL ASINRNEKNY FGSHPTEFGP DSGVSTGVMT LRKKLLQVLE QQMSSKLNET TEAIQRELEE TTYQFKVQYN EQPMSAESYL AASLDDFKHQ FHEFASSFGR PQLQTLLKDA LDQKVLDQLA ARYWNRPIED LSPAPREPDN IIDLPKADPD SPYWHRQLDT ACSGLTRLGV GRLAATVAAS AIQQHVEKLL DKSSFAKHPS ARKVISDAAA TVLADRSYAT SDGIEISLKP YKFDPDIQPN EWAQGREHVV GVLQAELEQC QAAMKALENS VGGRKKLKEV MSFVDKARKG EIIVEGDHPS GAGGFSAALL ARGREAVFLR DRADILSLRI QAAKSRQCKT LTNKYYCPEV FLDAVATKLA QTAVLFLNVE MLNDFYVRFP REVEAKLHEH MHAGGGLEKF AREDPKVRRH LDLIRRKELL ETVLGKIEEL HRISSGT

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Experimental details

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Structure determination

Methodcryo EM
Processingsubtomogram averaging
Aggregation stateparticle

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Sample preparation

Concentration5 mg/mL
BufferpH: 7.4 / Details: 20 mM HEPES, 200 mM NaCl, residual MgCl2, 9mM KCl.
GridModel: Quantifoil R2/2 / Material: COPPER / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE / Chamber humidity: 70 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV
DetailsSample was prepared in the described buffer. Just before freezing 6 nm colloidal gold fiducial marker were added to the sample in a 1:1 ratio.

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Specialist opticsEnergy filter - Slit width: 20 eV
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Average electron dose: 2.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 4.0 µm / Nominal defocus min: 2.0 µm / Nominal magnification: 53000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 20.4 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: Dynamo (ver. 1.1.266) / Number subtomograms used: 1677
ExtractionNumber tomograms: 1 / Number images used: 2214
Reference model: global average of the particles rotated to the known initial orientations
Method: Geometry-assisted particle picking form tube surfaces
Software - Name: Dynamo (ver. 1.1.266) / Details: with the use of Dynamo Catalogue system
CTF correctionSoftware:
Namedetails
Gctf (ver. 1.06)detection
IMOD (ver. 4.10)correction

Details: CTF determination was done by Gctf and correction was performed by ctfphaseflip from IMOD
Final 3D classificationNumber classes: 1 / Avg.num./class: 1677 / Software - Name: Dynamo (ver. 1.1.266)
Final angle assignmentType: OTHER / Software - Name: Dynamo (ver. 1.1.266) / Software - details: independent half-set refinement
Details: subtomogram averaging by cross correlation maximization
FSC plot (resolution estimation)

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