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Yorodumi- EMDB-71327: Cryo-EM structure of chimeric immunoglobulin M comprising bony fi... -
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Open data
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Basic information
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| Title | Cryo-EM structure of chimeric immunoglobulin M comprising bony fish and human sequences, hFcm-tFcm-chi4 | |||||||||
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Sample |
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Keywords | immunoglobulin M / fragment crystallization / IMMUNE SYSTEM | |||||||||
| Biological species | Homo sapiens (human) / ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.92 Å | |||||||||
Authors | Lyu M / Stadtmueller BM | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: bioRxiv / Year: 2025Title: Chimeric Immunoglobulin and human Immunoglobulin M structures provide insights on joining-chain independent assembly and function. Authors: Mengfan Lyu / Beth M Stadtmueller / ![]() Abstract: Polymeric (p) immunoglobulins (Igs) play critical roles in vertebrate immunity. IgM is the evolutionarily oldest pIg and functions both in circulation and in the mucosa. pIgM typically comprises ...Polymeric (p) immunoglobulins (Igs) play critical roles in vertebrate immunity. IgM is the evolutionarily oldest pIg and functions both in circulation and in the mucosa. pIgM typically comprises between four and six IgM monomers and up to one joining chain (JC), which in mammals facilitates pIg assembly and promotes delivery to mucosal secretions. Bony fish (teleosts) lack JC and assemble tetrameric IgM whereas humans can express JC-containing pentamers and JC-free hexamers. Here we report cryo-electron microscopy structures of two JC-free chimeric IgM, comprising bony fish and human sequences, and the structure of human hexameric IgM. Chimeric IgM structures adopted unique pentameric geometry distinct from both human and fish pIgM whereas the human hexameric IgM structure adopted hexagonal geometry similar to JC-containing pentameric IgM, albeit with structural differences in center of the molecule. Together results provide new insights on how IgM heavy chain motifs contribute to JC-free pIgM assembly and reveal plasticity of this process, which can be manipulated to create pIg structures not observed in nature. Moreover, we found that antigen-targeting chimeric IgM could neutralize toxin cytotoxicity, indicating potential to engineer uniquely structured pIgs to prevent or treat disease. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_71327.map.gz | 230.2 MB | EMDB map data format | |
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| Header (meta data) | emd-71327-v30.xml emd-71327.xml | 19.3 KB 19.3 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_71327_fsc.xml | 18.3 KB | Display | FSC data file |
| Images | emd_71327.png | 133.9 KB | ||
| Filedesc metadata | emd-71327.cif.gz | 6.3 KB | ||
| Others | emd_71327_half_map_1.map.gz emd_71327_half_map_2.map.gz | 226.4 MB 226.4 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-71327 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-71327 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_71327.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.058 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #1
| File | emd_71327_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_71327_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : pentameric chimeric immunoglobulin M-Fc comprising Oncorhynchus m...
| Entire | Name: pentameric chimeric immunoglobulin M-Fc comprising Oncorhynchus mykiss and human sequences |
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| Components |
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-Supramolecule #1: pentameric chimeric immunoglobulin M-Fc comprising Oncorhynchus m...
| Supramolecule | Name: pentameric chimeric immunoglobulin M-Fc comprising Oncorhynchus mykiss and human sequences type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 270 KDa |
-Macromolecule #1: Chimeric Immunoglobulin heavy constant mu
| Macromolecule | Name: Chimeric Immunoglobulin heavy constant mu / type: protein_or_peptide / ID: 1 Details: His-tagged chimeric IgM comprising Oncorhynchus mykiss and human sequences. Residues 343-546 are from human (Homo sapiens) and residues 547-575 are from rainbow trout (Oncorhynchus mykiss), hFcm-tFcm-chi4. Number of copies: 10 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 26.846229 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: HHHHHHSGTA IRVFAIPPSF ASIFLTKSTK LTCLVTDLTT YDSVTISWTR QNGEAVKTHT NISESHPNAT FSAVGEASIC EDDWNSGER FTCTVTHTDL PSPLKQTISR PKGVALHRPD VYLLPPAREQ LNLRESATIT CLVTGFSPAD VFVQWMQRGQ P LSPEKYVT ...String: HHHHHHSGTA IRVFAIPPSF ASIFLTKSTK LTCLVTDLTT YDSVTISWTR QNGEAVKTHT NISESHPNAT FSAVGEASIC EDDWNSGER FTCTVTHTDL PSPLKQTISR PKGVALHRPD VYLLPPAREQ LNLRESATIT CLVTGFSPAD VFVQWMQRGQ P LSPEKYVT SAPMPEPQAP GRYFAHSILT VSEEEWNTGE TYTCVVAHEA LPNRIIMRTI DRTSNQPNLV NLSLNVPQRC MA Q UniProtKB: Immunoglobulin heavy constant mu |
-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 | 0.2 mg/mL | |||||||||
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| Buffer | pH: 7.8 Component:
Details: 20mM Tris-HCl, 150mM NaCl, pH7.8 | |||||||||
| Grid | Model: Quantifoil R2/2 / Material: COPPER / Mesh: 400 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 90 sec. | |||||||||
| 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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| Software | Name: SerialEM |
| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number real images: 3341 / Average electron dose: 57.35 e/Å2 Details: Movies were collected on Titan Krios G4 Cryo-TEM (Thermo Fisher) operating at 300kV. 1679 movies were recorded on untilted stage whereas 1662 movies were recored on 30 degree tilted stage. ...Details: Movies were collected on Titan Krios G4 Cryo-TEM (Thermo Fisher) operating at 300kV. 1679 movies were recorded on untilted stage whereas 1662 movies were recored on 30 degree tilted stage. All movies were recorded using SerialEM on a post-GIF K3 Direct Electron Detector (Gatan) with 57.35 e/A2 total dose. |
| 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: 3.0 µm / Nominal defocus min: 0.5 µm |
| Sample stage | Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Refinement | Protocol: AB INITIO MODEL / Target criteria: Cross-correlation coefficient |
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| Output model | ![]() PDB-9p6v: |
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About Yorodumi



Keywords
Homo sapiens (human)
Authors
United States, 1 items
Citation

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FIELD EMISSION GUN

