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Yorodumi- EMDB-76887: Septin tetrameric complex from Caenorhabditis elegans by Cryo-EM -
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Open data
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Basic information
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| Title | Septin tetrameric complex from Caenorhabditis elegans by Cryo-EM | |||||||||
Map data | Map sharpening | |||||||||
Sample |
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Keywords | GTPase / Cytoskeleton component / CELL CYCLE | |||||||||
| Function / homology | Function and homology informationegg-laying behavior / septin complex / cytoskeleton-dependent cytokinesis / septin ring / post-embryonic development / locomotion / cell division site / cleavage furrow / intracellular protein localization / microtubule cytoskeleton ...egg-laying behavior / septin complex / cytoskeleton-dependent cytokinesis / septin ring / post-embryonic development / locomotion / cell division site / cleavage furrow / intracellular protein localization / microtubule cytoskeleton / midbody / molecular adaptor activity / cytoskeleton / GTPase activity / GTP binding Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.65 Å | |||||||||
Authors | Saladino GCR / Ciol H / Mendonca DC / Furtado AA / Pereira HM / Klaholz B / Araujo APU / Garratt RC | |||||||||
| Funding support | Brazil, 1 items
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Citation | Journal: J Mol Biol / Year: 2026Title: Cryo-EM Structure of the C. Elegans Septin Tetramer Reveals a Revised Architecture and Conserved Positional Orthology. Authors: Giovanna Christe Dos Reis Saladino / Heloísa Ciol / Deborah Cezar Mendonça / Adriano Alves Furtado / Humberto D'Muniz Pereira / Bruno P Klaholz / Ana Paula Ulian Araujo / Richard Charles Garratt / ![]() Abstract: Septins are cytoskeletal proteins that assemble into hetero-oligomeric complexes, which polymerize into filaments to regulate many cellular processes, including cytokinesis and membrane remodeling. ...Septins are cytoskeletal proteins that assemble into hetero-oligomeric complexes, which polymerize into filaments to regulate many cellular processes, including cytokinesis and membrane remodeling. In Caenorhabditis elegans, the core septin complex is a tetramer composed of two copies each of two different subunits, UNC-59 and UNC-61. Historically, low-resolution models suggested a subunit order of UNC-59-UNC-61-UNC-61-UNC-59 for the tetramer. However, this arrangement contradicted the positional conservation of septins observed in other species. Using cryo-EM, we obtained a structure for the tetramer with a global resolution of 2.7 Å, definitively establishing the subunit order to be UNC-61-UNC-59-UNC-59-UNC-61. This places UNC-59 at the center of the particle where it forms a homodimeric G-interface, confirming it to be a positional ortholog of human SEPT7. This arrangement is further supported by mutational/biophysical analyses. Despite the stability of the tetramer, the complex failed to polymerize into filaments in vitro, which we attribute to the structural instability of the terminal UNC-61 G-interfaces. Our results suggest that post-translational modifications or specific cellular factors may be required to initiate higher-order assembly in C. elegans. Furthermore, our structure reveals that while UNC-59 possesses key characteristics of the SEPT7 group, it also features unique structural adaptations that may be related to the unique arrangement of the C. elegans complex. We demonstrate that the previous misidentification of the subunit order within the tetramer likely stemmed from N-terminal domain swapping, reinforcing the importance of high-resolution structural studies for understanding the evolutionary history and the diversity of septins. | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_76887.map.gz | 483.9 MB | EMDB map data format | |
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| Header (meta data) | emd-76887-v30.xml emd-76887.xml | 20.9 KB 20.9 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_76887_fsc.xml | 16.9 KB | Display | FSC data file |
| Images | emd_76887.png | 64.2 KB | ||
| Masks | emd_76887_msk_1.map | 512 MB | Mask map | |
| Filedesc metadata | emd-76887.cif.gz | 6.9 KB | ||
| Others | emd_76887_half_map_1.map.gz emd_76887_half_map_2.map.gz | 475.7 MB 475.7 MB | ||
| Archive directory | https://data.pdbj.org/pub/emdb/structures/EMD-76887 ftp://data.pdbj.org/pub/emdb/structures/EMD-76887 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 12znMC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_76887.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Map sharpening | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.729 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_76887_msk_1.map | ||||||||||||
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| Density Histograms |
-Half map: Half map B
| File | emd_76887_half_map_1.map | ||||||||||||
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| Annotation | Half map B | ||||||||||||
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| Density Histograms |
-Half map: Half map A
| File | emd_76887_half_map_2.map | ||||||||||||
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| Annotation | Half map A | ||||||||||||
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Sample components
-Entire : Heterotetramer of C. elegans septins (UNC-61 - UNC-59 - UNC-59 - ...
| Entire | Name: Heterotetramer of C. elegans septins (UNC-61 - UNC-59 - UNC-59 - UNC-61) |
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| Components |
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-Supramolecule #1: Heterotetramer of C. elegans septins (UNC-61 - UNC-59 - UNC-59 - ...
| Supramolecule | Name: Heterotetramer of C. elegans septins (UNC-61 - UNC-59 - UNC-59 - UNC-61) type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 209.31 KDa |
-Macromolecule #1: Septin
| Macromolecule | Name: Septin / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 53.135703 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MMSDIEHKLQ HLPPHQPPPP VPHHHQNQPT HNNTTTISSA TSSINTTTTS KKPTIAAPTA PSPIKSLSDH TGRVMQLNGH VGFDSLPHQ LVKKAVEAGF QFNLMCVGET GTGKTTLIES LFNMKLDFEP CNHELKTVEL RTCTKDVAEG GIRVKLRLVE T AGFGDQLD ...String: MMSDIEHKLQ HLPPHQPPPP VPHHHQNQPT HNNTTTISSA TSSINTTTTS KKPTIAAPTA PSPIKSLSDH TGRVMQLNGH VGFDSLPHQ LVKKAVEAGF QFNLMCVGET GTGKTTLIES LFNMKLDFEP CNHELKTVEL RTCTKDVAEG GIRVKLRLVE T AGFGDQLD KDKSAKVIVD YLESQFETYL QEELKPRRML QYFNDSRIHA CLYFISPTGH GLKALDLVTL RELAKRVNVI PV IAKSDTT CKDELLRFKA KILSELKSQK IDIYTFPTDD ETVSTTNKEM NKSVPFAVVG SIDFVKKENG QMVRARQYPW GIV EVENES HCDFVKLREA LLRTNVDEMR QRTHESLYEN YRRDRLRQMK IGDGETGPKI IEKLAQKHRE HQDEFSRREL TLRE EFQKK LDVTEGDMRK VEEGLAARER EVHENYNREA SKLDMEIRQL TEERMKLMTK VSKKLRK UniProtKB: Septin |
-Macromolecule #2: Septin
| Macromolecule | Name: Septin / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 55.299492 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MGMHHHHHHE NLYFQGSQDP SSRTANSSSR NDESLRTGQH KENPNYWGFA NFPNQVFRRA VKNGFDFTLM VVGRSGLGKS TFINTLFLA EINNLNEKES APTHPHPSTV RVEEKLVKLV ENSVSLNLTL VDTPGFGDAV NNSKCWEPIV NYVESKFFEQ F CEETRIDR ...String: MGMHHHHHHE NLYFQGSQDP SSRTANSSSR NDESLRTGQH KENPNYWGFA NFPNQVFRRA VKNGFDFTLM VVGRSGLGKS TFINTLFLA EINNLNEKES APTHPHPSTV RVEEKLVKLV ENSVSLNLTL VDTPGFGDAV NNSKCWEPIV NYVESKFFEQ F CEETRIDR GEKIVDKCVH LCLYFIEPSG HGLKPIDIEL MKHLHGRVNI VPVISKADCL TRDELLRFKK QIVKDAETAE IK LYKFPEL EDPYTDKVAI EKLRKALPFA IIGSNMLKEK DGKKIRYREY PWGTVEVENM QHNDFLTLRD MIIRTNLIDM IDV TRNVHY ENFRFRQMEG LPKNEKNRDP FTHLEEERRQ KEQDLDEKRN TLEKVFTEKT SARKKRSDER MSALEELEQQ NKQK IDAKR AEIIRLRHEI SELKNGNLTS SQTSLAMYNE NNHSQNSTLN STTKSSPPPT SATSSSSGTM KKRMGGLGLF NRN UniProtKB: Septin |
-Macromolecule #3: GUANOSINE-5'-DIPHOSPHATE
| Macromolecule | Name: GUANOSINE-5'-DIPHOSPHATE / type: ligand / ID: 3 / Number of copies: 2 / Formula: GDP |
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| Molecular weight | Theoretical: 443.201 Da |
| Chemical component information | ![]() ChemComp-GDP: |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 0.7 mg/mL | ||||||||||||
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| Buffer | pH: 7.5 Component:
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| Grid | Model: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE | ||||||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Number real images: 5998 / Average electron dose: 44.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 165000 |
| Sample stage | Specimen 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
-Atomic model buiding 1
| Initial model |
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| Refinement | Space: REAL / Protocol: RIGID BODY FIT | ||||||
| Output model | ![]() PDB-12zn: |
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Keywords
Authors
Brazil, 1 items
Citation

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FIELD EMISSION GUN

