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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | 1C5H TCR bound to R-phycoerythrin | |||||||||
Map data | Composite Map | |||||||||
Sample |
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Keywords | T-cell / gamma delta TCR / phycoerythrin / direct / IMMUNE SYSTEM | |||||||||
| Function / homology | Phycobilisome, alpha/beta subunit / Phycobilisome, alpha/beta subunit superfamily / Phycobilisome protein / phycobilisome / chloroplast thylakoid membrane / photosynthesis / Globin-like superfamily / R-phycoerythrin class I beta subunit / R-phycoerythrin class I alpha subunit Function and homology information | |||||||||
| Biological species | Homo sapiens (human) / Ceramium secundatum (eukaryote) / Pyropia tenera (asakusa nori) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.03 Å | |||||||||
Authors | Rashleigh L / Venugopal H / Rossjohn J / Gully BS | |||||||||
| Funding support | Australia, 1 items
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Citation | Journal: Structure / Year: 2025Title: Antibody-like recognition of a γδ T cell receptor toward a foreign antigen. Authors: Liam Rashleigh / Hariprasad Venugopal / Michael T Rice / Sachith D Gunasinghe / Chhon Ling Sok / Nicholas A Gherardin / Catarina F Almeida / Ildiko Van Rhijn / D Branch Moody / Dale I ...Authors: Liam Rashleigh / Hariprasad Venugopal / Michael T Rice / Sachith D Gunasinghe / Chhon Ling Sok / Nicholas A Gherardin / Catarina F Almeida / Ildiko Van Rhijn / D Branch Moody / Dale I Godfrey / Jamie Rossjohn / Benjamin S Gully / ![]() Abstract: The antigen recognition principles of B cells and αβ T cells have been well described compared to those of the γδ T cell. By way of their specificity conferring receptor (γδTCR), γδ T cells ...The antigen recognition principles of B cells and αβ T cells have been well described compared to those of the γδ T cell. By way of their specificity conferring receptor (γδTCR), γδ T cells can directly bind proteinaceous antigens. A known γδ T cell and B cell model antigen is phycoerythrin (PE), a light harvesting protein from rhodophytes and cyanobacteria. Here we probed human γδTCR reactivity to PE, in which a Vδ1Vγ5 TCR bound directly to induce proximal signaling and cellular activation. We determined the cryoelectron microscopy (cryo-EM) structure of the γδTCR-phycoerythrin immune complex. We then determined the cryo-EM structures of an antibody fragment and an αβTCR bound to PE. This revealed convergent use of apical aromatic residues to mediate contacts with a common PE epitope. Comparative analyses of the γδTCR revealed multiple antibody-like characteristics, including an enrichment of apical aromatic residues. Our findings reveal further distinct facets of antigen recognition by the γδTCR. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_70157.map.gz | 161.6 MB | EMDB map data format | |
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| Header (meta data) | emd-70157-v30.xml emd-70157.xml | 18.4 KB 18.4 KB | Display Display | EMDB header |
| Images | emd_70157.png | 90.5 KB | ||
| Filedesc metadata | emd-70157.cif.gz | 6.3 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-70157 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-70157 | HTTPS FTP |
-Validation report
| Summary document | emd_70157_validation.pdf.gz | 589.2 KB | Display | EMDB validaton report |
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| Full document | emd_70157_full_validation.pdf.gz | 588.8 KB | Display | |
| Data in XML | emd_70157_validation.xml.gz | 7.1 KB | Display | |
| Data in CIF | emd_70157_validation.cif.gz | 8.3 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-70157 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-70157 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9o62MC ![]() 9mgbC ![]() 9mkoC ![]() 9o60C ![]() 9o61C C: citing same article ( M: atomic model generated by this map |
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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_70157.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Composite Map | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.82 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : 1C5H TCR bound to R-phycoerythrin
| Entire | Name: 1C5H TCR bound to R-phycoerythrin |
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| Components |
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-Supramolecule #1: 1C5H TCR bound to R-phycoerythrin
| Supramolecule | Name: 1C5H TCR bound to R-phycoerythrin / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4 |
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| Source (natural) | Organism: Homo sapiens (human) |
-Supramolecule #2: R-phycoerythrin
| Supramolecule | Name: R-phycoerythrin / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#2 |
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| Source (natural) | Organism: Ceramium secundatum (eukaryote) |
-Supramolecule #3: 1C5H TCR
| Supramolecule | Name: 1C5H TCR / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #3-#4 |
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| Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: R-phycoerythrin class I alpha subunit
| Macromolecule | Name: R-phycoerythrin class I alpha subunit / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO |
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| Source (natural) | Organism: Pyropia tenera (asakusa nori) |
| Molecular weight | Theoretical: 17.707906 KDa |
| Sequence | String: MKSVITTTIS AADAAGRFPS SSDLESVQGN IQRAASRLEA AEKLAGNHEA VVKEAGDACF AKYPYLKNPG EAGDSQEKIN KCYRDIDHY MRLINYSLVV GGTGPLDEWG IAGAREVYRA LNLPGSSYIA AFVFTRDRLC VPRDMSAQAA VEFSGALDYV I NSLC UniProtKB: R-phycoerythrin class I alpha subunit |
-Macromolecule #2: R-phycoerythrin class I beta subunit
| Macromolecule | Name: R-phycoerythrin class I beta subunit / type: protein_or_peptide / ID: 2 / Number of copies: 6 / Enantiomer: LEVO |
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| Source (natural) | Organism: Pyropia tenera (asakusa nori) |
| Molecular weight | Theoretical: 18.33685 KDa |
| Sequence | String: MLDAFSRVVV NSDSKAAYVS GSDLQALKTF IADGNKRLDA VNSIVSNASC IVSDAVSGMI CENPGLIAPG GNCYTNRRMA ACLRDGEII LRYTSYALLA GDSSVLEDRC LNGLKETYIA LGVPTNSTAR AVSIMKSSAV AFISNTAPQR KMATAAGDCS A LSSEVASY CDKVSAAI UniProtKB: R-phycoerythrin class I beta subunit |
-Macromolecule #3: 1C5H TCR delta chain
| Macromolecule | Name: 1C5H TCR delta chain / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 26.886508 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: AQKVTQAQSS VSMPVRKAVT LNCLYETSWW SYYIFWYKQL PSKEMIFLIR QGSDEQNAKS GRYSVNFKKA AKSVALTISA LQLEDSAKY FCALGAPHTY WGISTDLSSW DTRQMFFGTG IKLFVEPRSQ PHTKPSVFVM KNGTNVACLV KEFYPKDIRI N LVSSKKIT ...String: AQKVTQAQSS VSMPVRKAVT LNCLYETSWW SYYIFWYKQL PSKEMIFLIR QGSDEQNAKS GRYSVNFKKA AKSVALTISA LQLEDSAKY FCALGAPHTY WGISTDLSSW DTRQMFFGTG IKLFVEPRSQ PHTKPSVFVM KNGTNVACLV KEFYPKDIRI N LVSSKKIT EFDPAIVISP SGKYNAVKLG KYEDSNSVTC SVQHDNKTVH STDFEVKTDS TDHVKPKETE NTKQPSKSAS G |
-Macromolecule #4: TCR gamma chain
| Macromolecule | Name: TCR gamma chain / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 27.014568 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: SSNLEGGTKS VTRPTRSSAE ITCDLTVINA FYIHWYLHQE GKAPQRLLYY DVSNSKDVLE SGLSPGKYYT HTPRRWSWIL ILRNLIEND SGVYYCATWD RPSKLFGSGT TLVVTDKQLD ADVSPKPTIF LPSIAETKLQ KAGTYLCLLE KFFPDVIKIH W QEKKSNTI ...String: SSNLEGGTKS VTRPTRSSAE ITCDLTVINA FYIHWYLHQE GKAPQRLLYY DVSNSKDVLE SGLSPGKYYT HTPRRWSWIL ILRNLIEND SGVYYCATWD RPSKLFGSGT TLVVTDKQLD ADVSPKPTIF LPSIAETKLQ KAGTYLCLLE KFFPDVIKIH W QEKKSNTI LGSQEGNTMK TNDTYMKFSW LTVPEESLDK EHRCIVRHEN NKNGVDQEII FPPIKTDVIT MDPKDNASG |
-Macromolecule #5: PHYCOERYTHROBILIN
| Macromolecule | Name: PHYCOERYTHROBILIN / type: ligand / ID: 5 / Number of copies: 24 / Formula: PEB |
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| Molecular weight | Theoretical: 588.694 Da |
| Chemical component information | ![]() ChemComp-PEB: |
-Macromolecule #6: PHYCOUROBILIN
| Macromolecule | Name: PHYCOUROBILIN / type: ligand / ID: 6 / Number of copies: 6 / Formula: PUB |
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| Molecular weight | Theoretical: 590.71 Da |
| Chemical component information | ![]() ChemComp-CYB: |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 8.5 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.4 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Homo sapiens (human)
Ceramium secundatum (eukaryote)
Authors
Australia, 1 items
Citation












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Processing
FIELD EMISSION GUN
