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- EMDB-40217: CryoEM map of the locally refined cardiolipin containing monolaye... -
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Basic information
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Title | CryoEM map of the locally refined cardiolipin containing monolayer and soluble OPA1 paddles from the GDP-AlFx bound helical assembly on a lipid membrane | |||||||||
![]() | CryoEM map of the locally refined cardiolipin containing monolayer and soluble OPA1 from the GDP-AlFx bound helical assembly on a lipid membrane | |||||||||
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![]() | GTPase / Dynamin-family protein / mitochondrial fusion protein / mitochondria / Optic Atrophy / LIPID BINDING PROTEIN | |||||||||
Function / homology | ![]() Regulation of Apoptosis / mitochondrial inner membrane fusion / membrane tubulation / GTPase-dependent fusogenic activity / membrane bending activity / inner mitochondrial membrane organization / dynamin GTPase / cristae formation / mitochondrial genome maintenance / phosphatidic acid binding ...Regulation of Apoptosis / mitochondrial inner membrane fusion / membrane tubulation / GTPase-dependent fusogenic activity / membrane bending activity / inner mitochondrial membrane organization / dynamin GTPase / cristae formation / mitochondrial genome maintenance / phosphatidic acid binding / mitochondrial fission / cardiolipin binding / positive regulation of T-helper 17 cell lineage commitment / GTP metabolic process / mitochondrial fusion / axonal transport of mitochondrion / negative regulation of release of cytochrome c from mitochondria / mitochondrial crista / positive regulation of interleukin-17 production / negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / axon cytoplasm / visual perception / mitochondrion organization / Mitochondrial protein degradation / neural tube closure / mitochondrial membrane / cellular senescence / mitochondrial intermembrane space / protein complex oligomerization / microtubule binding / mitochondrial outer membrane / microtubule / mitochondrial inner membrane / GTPase activity / dendrite / negative regulation of apoptotic process / GTP binding / apoptotic process / magnesium ion binding / mitochondrion / nucleoplasm / membrane / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | helical reconstruction / cryo EM / Resolution: 2.91 Å | |||||||||
![]() | Nyenhuis SB / Wu X / Strub MP / Yim YI / Stanton AE / Baena V / Syed ZA / Canagarajah B / Hammer JA / Hinshaw JE | |||||||||
Funding support | ![]()
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![]() | ![]() Title: OPA1 helical structures give perspective to mitochondrial dysfunction. Authors: Sarah B Nyenhuis / Xufeng Wu / Marie-Paule Strub / Yang-In Yim / Abigail E Stanton / Valentina Baena / Zulfeqhar A Syed / Bertram Canagarajah / John A Hammer / Jenny E Hinshaw / ![]() Abstract: Dominant optic atrophy is one of the leading causes of childhood blindness. Around 60-80% of cases are caused by mutations of the gene that encodes optic atrophy protein 1 (OPA1), a protein that has ...Dominant optic atrophy is one of the leading causes of childhood blindness. Around 60-80% of cases are caused by mutations of the gene that encodes optic atrophy protein 1 (OPA1), a protein that has a key role in inner mitochondrial membrane fusion and remodelling of cristae and is crucial for the dynamic organization and regulation of mitochondria. Mutations in OPA1 result in the dysregulation of the GTPase-mediated fusion process of the mitochondrial inner and outer membranes. Here we used cryo-electron microscopy methods to solve helical structures of OPA1 assembled on lipid membrane tubes, in the presence and absence of nucleotide. These helical assemblies organize into densely packed protein rungs with minimal inter-rung connectivity, and exhibit nucleotide-dependent dimerization of the GTPase domains-a hallmark of the dynamin superfamily of proteins. OPA1 also contains several unique secondary structures in the paddle domain that strengthen its membrane association, including membrane-inserting helices. The structural features identified in this study shed light on the effects of pathogenic point mutations on protein folding, inter-protein assembly and membrane interactions. Furthermore, mutations that disrupt the assembly interfaces and membrane binding of OPA1 cause mitochondrial fragmentation in cell-based assays, providing evidence of the biological relevance of these interactions. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 239.1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.1 KB 17.1 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 16.5 KB | Display | ![]() |
Images | ![]() | 105.4 KB | ||
Masks | ![]() | 476.8 MB | ![]() | |
Others | ![]() ![]() | 443 MB 443 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8eewC ![]() 8ef7C ![]() 8effC ![]() 8efrC ![]() 8efsC ![]() 8eftC C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Map
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Annotation | CryoEM map of the locally refined cardiolipin containing monolayer and soluble OPA1 from the GDP-AlFx bound helical assembly on a lipid membrane | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.2018 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Projections & Slices |
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Density Histograms |
-Half map: CryoEM half map A of the locally refined...
File | emd_40217_half_map_1.map | ||||||||||||
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Annotation | CryoEM half map A of the locally refined cardiolipin containing monolayer and soluble OPA1 from the GDP-AlFx bound helical assembly on a lipid membrane | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: CryoEM half map B of the locally refined...
File | emd_40217_half_map_2.map | ||||||||||||
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Annotation | CryoEM half map B of the locally refined cardiolipin containing monolayer and soluble OPA1 from the GDP-AlFx bound helical assembly on a lipid membrane | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : sOPA1 helical assembly on a lipid membrane
Entire | Name: sOPA1 helical assembly on a lipid membrane |
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Components |
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-Supramolecule #1: sOPA1 helical assembly on a lipid membrane
Supramolecule | Name: sOPA1 helical assembly on a lipid membrane / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: sOPA1 protein
Macromolecule | Name: sOPA1 protein / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: ATDRGSESDK HFRKVSDKEK IDQLQEELLH TQLKYQRILE RLEKENKELR KLVLQKDDKG IHHRKLKKSL IDMYSEVLD VLSDYDASYN TQDHLPRVVV VGDQSAGKTS VLEMIAQARI FPRGSGEMMT RSPVKVTLSE G PHHVALFK DSSREFDLTK EEDLAALRHE ...String: ATDRGSESDK HFRKVSDKEK IDQLQEELLH TQLKYQRILE RLEKENKELR KLVLQKDDKG IHHRKLKKSL IDMYSEVLD VLSDYDASYN TQDHLPRVVV VGDQSAGKTS VLEMIAQARI FPRGSGEMMT RSPVKVTLSE G PHHVALFK DSSREFDLTK EEDLAALRHE IELRMRKNVK EGCTVSPETI SLNVKGPGLQ RMVLVDLPGV IN TVTSGMA PDTKETIFSI SKAYMQNPNA IILCIQDGSV DAERSIVTDL VSQMDPHGRR TIFVLTKVDL AEK NVASPS RIQQIIEGKL FPMKALGYFA VVTGKGNSSE SIEAIREYEE EFFQNSKLLK TSMLKAHQVT TRNL SLAVS DCFWKMVRES VEQQADSFKA TRFNLETEWK NNYPRLRELD RNELFEKAKN EILDEVISLS QVTPK HWEE ILQQSLWERV STHVIENIYL PAAQTMNSGT FNTTVDIKLK QWTDKQLPNK AVEVAWETLQ EEFSRF MTE PKGKEHDDIF DKLKEAVKEE SIKRHKWNDF AEDSLRVIQH NALEDRSISD KQQWDAAIYF MEEALQA RL KDTENAIENM VGPDWKKRWL YWKNRTQEQC VHNETKNELE KMLKCNEEHP AYLASDEITT VRKNLESR G VEVDPSLIKD TWHQVYRRHF LKTALNHCNL CRRGFYYYQR HFVDSELECN DVVLFWRIQR MLAITANTL RQQLTNTEVR RLEKNVKEVL EDFAEDGEKK IKLLTGKRVQ LAEDLKKVRE IQEKLDAFIE ALHQEK UniProtKB: Dynamin-like GTPase OPA1, mitochondrial |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | helical reconstruction |
Aggregation state | helical array |
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Sample preparation
Buffer | pH: 7.2 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 0.3 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: FLEXIBLE FIT |
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