+
Open data
-
Basic information
Entry | ![]() | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Title | Cryo-EM structure of GD-BatCoV (BtCoV/Ii/GD/2014-422) S-trimer | ||||||||||||
![]() | |||||||||||||
![]() |
| ||||||||||||
![]() | spike protein / VIRAL PROTEIN | ||||||||||||
Function / homology | ![]() virion component / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / receptor-mediated virion attachment to host cell / endocytosis involved in viral entry into host cell / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / host cell plasma membrane / virion membrane / membrane Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() ![]() | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.1 Å | ||||||||||||
![]() | Yuan H / Xiong X / Gao X / Li Z / Wang J | ||||||||||||
Funding support | 3 items
| ||||||||||||
![]() | ![]() Title: Structures and receptor binding activities of merbecovirus spike proteins reveal key signatures for human DPP4 adaptation. Authors: Hang Yuan / Jingjing Wang / Yong Ma / Zimu Li / Xijie Gao / Gul Habib / Banghui Liu / Jing Chen / Jun He / Peng Zhou / Zheng-Li Shi / Xinwen Chen / Xiaoli Xiong / ![]() Abstract: Merbecoviruses from bats, pangolins, and hedgehogs pose significant zoonotic threats, with a limited understanding of receptor binding by their spike (S) proteins. Here, we report cryo-EM structures ...Merbecoviruses from bats, pangolins, and hedgehogs pose significant zoonotic threats, with a limited understanding of receptor binding by their spike (S) proteins. Here, we report cryo-EM structures of GD-BatCoV (BtCoV-422) and SE-PangolinCoV (MjHKU4r-CoV-1) RBDs in complex with human DPP4 (hDPP4). These structures exhibit a substantial offset in their hDPP4 interaction interfaces, revealing a conserved hydrophobic cluster as a convergent signature of DPP4 binding within the MERS-HKU4 clade of merbecoviruses. Structure-guided mutagenesis demonstrates that favorable interactions are distributed across multiple receptor binding motif (RBM) regions, working synergistically to confer high-affinity hDPP4 binding. Swapping of the merbecovirus RBM regions indicate limited plasticity and interchangeability among these regions. In addition, we report cryo-EM structures of six merbecovirus S-trimers. Structure-based phylogenetics suggests that hDPP4-binding merbecoviruses undergo convergent evolution, while ACE2-binding merbecoviruses exhibit diversification in their binding mechanisms. These findings offer critical insights into merbecovirus receptor utilization, providing a structural understanding for future surveillance. | ||||||||||||
History |
|
-
Structure visualization
Supplemental images |
---|
-
Downloads & links
-EMDB archive
Map data | ![]() | 117.2 MB | ![]() | |
---|---|---|---|---|
Header (meta data) | ![]() ![]() | 19.9 KB 19.9 KB | Display Display | ![]() |
Images | ![]() | 8 KB | ||
Filedesc metadata | ![]() | 7.2 KB | ||
Others | ![]() ![]() | 98.4 MB 98.4 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 869.6 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 869.2 KB | Display | |
Data in XML | ![]() | 14 KB | Display | |
Data in CIF | ![]() | 16.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9jmpMC ![]() 9jmfC ![]() 9jmgC ![]() 9jmhC ![]() 9jmiC ![]() 9jmjC ![]() 9jmmC ![]() 9jmnC ![]() 9jmoC M: atomic model generated by this map C: citing same article ( |
---|---|
Similar structure data | Similarity search - Function & homology ![]() |
-
Links
EMDB pages | ![]() ![]() |
---|---|
Related items in Molecule of the Month |
-
Map
File | ![]() | ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.32 Å | ||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
|
-Supplemental data
-Half map: #2
File | emd_61609_half_map_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: #1
File | emd_61609_half_map_2.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-
Sample components
-Entire : BatCoV (BtCoV/Ii/GD/2014-422) Spike protein
Entire | Name: BatCoV (BtCoV/Ii/GD/2014-422) Spike protein |
---|---|
Components |
|
-Supramolecule #1: BatCoV (BtCoV/Ii/GD/2014-422) Spike protein
Supramolecule | Name: BatCoV (BtCoV/Ii/GD/2014-422) Spike protein / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: #1 |
---|---|
Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Spike glycoprotein,Fibritin
Macromolecule | Name: Spike glycoprotein,Fibritin / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 151.326953 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MRLSVCLLMF LLTPIKGDVD SGPPSSATSC KEADMRNSSS EFFNKQWPMP INASKADGII YPTGKSYSNI SLTLQGLFPK HGDLGEQYI YSVGHSDSNY DYLGKLFVSD YATKVVPFNN GFVVRIGAAA NATGSVIIST VQKTIKKIYP AFMLGSSVGN F SNGVSGRY ...String: MRLSVCLLMF LLTPIKGDVD SGPPSSATSC KEADMRNSSS EFFNKQWPMP INASKADGII YPTGKSYSNI SLTLQGLFPK HGDLGEQYI YSVGHSDSNY DYLGKLFVSD YATKVVPFNN GFVVRIGAAA NATGSVIIST VQKTIKKIYP AFMLGSSVGN F SNGVSGRY FNHTLLLLPD GCGTRLWALY CVIEPRNGSY CPGNSNYNTF AVFDTPHTDC TSAGYNTNAT LNSFKEYFDL QN CSFIYSF NITEDENAEW FGITQNTQGV HLYSSRKGDL YGSNMFLFAT LPVYDGIKYY TVIPRSIRSK YSERQAWAAF YIY SLHKLT YLLDFSVDGY IRRAVDCGHD DLSQLYCSYE SFDVGSGVYS VSSFEVHSRG QFIEQPNSVE CDFTKLLSGT PPQV YNFNR LVFTNCNYNL TKLLSLFMVN EFSCDGISPD AIARGCYSSL TVDYFAYPLS MKSYMQPGSA GVISQYNYKQ SFANP TCRI FATAPANLTI TKPSSYSFIS KCSRLTGDNS HIETPIVINP GEYSICKNFA PNGFSQDGDY FTRQLSQLEG GGILVG VGS VTPMTDTLQM GFIISVQYGT DTNSVCPMMD LGNSTTITDK LGVCVEYNLY GVSGRGVFIN CTAVGVKQQR FVYDGFD NL IGYYSDDGNY YCVRPCVSVP LSVVYDKTTN SHATIFGSVA CEHITTMLHQ FSRTTQASLR MRDVSNSGPL QTAVGCVI G LVNSSMVVDN CQLPLGQSLC AVPSTTRSSS QLQLATINYT QPQLLSPLNS SGFVVQVPTN FSFGITQEYI QTTIQKVTV DCKQYVCNGF QKCEQLLREY GQFCAKINQA LHGANLMQDE SVANLFSDIK THKSQPLNAG LNGDFNLTLL QVPQVSTSQY SHRSPIEDL LFNKVTIADP GYMQGYDDCM KQGPPSARDL ICAQYVAGYK VLPPLYDPNM EGAYTSSLLG SIAGAGWTAG L SPFAAIPF PQSIFYRMNG IGITQQVLSE NQKLIANKFN QALGAMQTGF TTTPLAFSKV QDAVNANAQA LSKLASELSN TF GAISSSI SDILKRLDPP EQEAQIDRLI NGRLTSLNAF VAQQLVRSET AARSAQLASD KVNECVKSQS KRNGFCGSGT HIV SFVINA PNGFYFFHVG YVPTNHVNVT AAYGLCNTDT PPRCIAPIDG YFVLNNTTTR DVVDQWYYTG SSFFNPEPIT MANA RYVSQ DVKFENLTNQ LPPPLLNNQT DLDFKEELEE FFKNVSSQGP NFQEISKINT TLLDLSTEMK VLNEVVKQLN ESYID LKEL GNYSYYQKWP GSGYIPEAPR DGQAYVRKDG EWVLLSTFLL EVLFQGPGHH HHHHHHSAWS HPQFEKGGGS GGGGSG GSA WSHPQFEKSA UniProtKB: Spike glycoprotein, Fibritin |
-Macromolecule #4: 2-acetamido-2-deoxy-beta-D-glucopyranose
Macromolecule | Name: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 4 / Number of copies: 21 / Formula: NAG |
---|---|
Molecular weight | Theoretical: 221.208 Da |
Chemical component information | ![]() ChemComp-NAG: |
-Macromolecule #5: LINOLEIC ACID
Macromolecule | Name: LINOLEIC ACID / type: ligand / ID: 5 / Number of copies: 3 / Formula: EIC |
---|---|
Molecular weight | Theoretical: 280.445 Da |
Chemical component information | ![]() ChemComp-EIC: |
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
![]() | single particle reconstruction |
Aggregation state | particle |
-
Sample preparation
Buffer | pH: 7.4 |
---|---|
Vitrification | Cryogen name: ETHANE |
-
Electron microscopy
Microscope | FEI TALOS ARCTICA |
---|---|
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: ![]() |
Electron optics | Illumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.8 µm |
Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |