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- EMDB-61600: Cryo-EM structure of SA-BatCoV (Neoromicia/PML-PHE1/RSA/2011) S-trimer -
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Open data
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Basic information
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Title | Cryo-EM structure of SA-BatCoV (Neoromicia/PML-PHE1/RSA/2011) S-trimer | ||||||||||||
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![]() | 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 | ||||||||||||
Funding support | 3 items
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![]() | ![]() 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 |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 49.5 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 20.3 KB 20.3 KB | Display Display | ![]() |
Images | ![]() | 18.7 KB | ||
Filedesc metadata | ![]() | 7 KB | ||
Others | ![]() ![]() | 40.8 MB 40.8 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 892.1 KB | Display | ![]() |
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Full document | ![]() | 891.6 KB | Display | |
Data in XML | ![]() | 11.7 KB | Display | |
Data in CIF | ![]() | 13.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9jmfMC ![]() 9jmgC ![]() 9jmhC ![]() 9jmiC ![]() 9jmjC ![]() 9jmmC ![]() 9jmnC ![]() 9jmoC ![]() 9jmpC M: atomic model generated by this map 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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Related items in Molecule of the Month |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.32 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_61600_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_61600_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : SA-BatCoV (Neoromicia/PML-PHE1/RSA/2011) Spike protein
Entire | Name: SA-BatCoV (Neoromicia/PML-PHE1/RSA/2011) Spike protein |
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Components |
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-Supramolecule #1: SA-BatCoV (Neoromicia/PML-PHE1/RSA/2011) Spike protein
Supramolecule | Name: SA-BatCoV (Neoromicia/PML-PHE1/RSA/2011) Spike protein type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 450 KDa |
-Macromolecule #1: Spike glycoprotein,Fibritin
Macromolecule | Name: Spike glycoprotein,Fibritin / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 150.804984 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MTYSVFPLMC LLTFIGANAK IVTLPGNDAT GYCPSVDMQP SYFIQHNWPE PIDMNKADGV IYPNGRTYSN ITLQTTNLFP KNGDLGTQY VYSASNHKST ANDAFISNYS YYGNPFGDGI VIRIGQNANK TGSVIVGQAQ TTMKKIYPAL MLGSSFGNFS A NNKSGAYF ...String: MTYSVFPLMC LLTFIGANAK IVTLPGNDAT GYCPSVDMQP SYFIQHNWPE PIDMNKADGV IYPNGRTYSN ITLQTTNLFP KNGDLGTQY VYSASNHKST ANDAFISNYS YYGNPFGDGI VIRIGQNANK TGSVIVGQAQ TTMKKIYPAL MLGSSFGNFS A NNKSGAYF NHTLLILPSK CGTVFQVAYC LLQPRTESKC PGNSNYVSYF LADSPSDCSS TSDEIRRNGL RDIRKFFNLV NC TYFEEFN VTADERAEWF GIVQDAQGVH LYTSRKNGFN SNNLFLFATV PIYDKLNYYT VIPRSVITPS NQRDAWAAFY IYP LHQLSY LLNFDVNGYI TQAADCGYND YTQLICSYGD FNMKSGVYST SYYSAKPVGA YYEAHVYPDC NFTELFRERA PTIM QYKRE VFTRCNYNLS LLLSLVQVDE FVCDKITPEA LATGCYSSLT VDWFAFPYAW KSYLAIGSAD RIVRFNYNQD YSNPS CRIH SKVNSSIGIS YAGAYSYITN CNYGATNKDD VVKPGGRASQ QCITGALNSP TTGQLWAYNF GGVPYRVSRL TYTDHL SDP LDMVYVITVK YEPGAETVCP KQIRPDYSTN ITHLLGSCIS YDIYGITGTG VFQLCNATGI RQQKFVYDKF DNIIGFH SD DGNYYCVAPC VSVPVSVIYD DKTNQYATLF GSVACQHIST MAAQFSRETR ASLVSRNMQN LLQTSVGCVM GFHETNDT V EECHLSLGQS LCAIPPNTNL RSGRSTFGLG SLAYNSPLRV DALNSSEFKV SLPLNFTFGV TQEYIETSIQ KITVDCKQY VCNGFAKCEK LLEQYGQFCS KINQALHGAN LRQDDSVRNL FESVKTPQTV PLTTGFGGEF NLTLLEPLSV STGSSNARSA LEELLFDSV TIADPGYMQG YDDCMQQGPA SARDLICAQY VAGYKVLPPL MDVNMEAAYT SSLLGSIAGA GWTAGLSSFA A IPFAQSIF YRLNGVGITQ QVLSENQKII ANKFNQALGA MQTGFTTTNE AFQKVQDAVN TNAQALAKLA SELSNTFGAI SS SIGDIIQ RLDVLEQEVQ IDRLINGRLT TLNAFVAQQL VRSESAARSA QLAKDKVNEC VKSQSTRSGF CGQGTHIVSF VIN APNGLY FMHVGYHPSQ HIEVVAAYGL CDSANPTNCI APVNGYFIKN QTTRSADEWS YTGSSFYAPE PITTLNTRYV APQV TFQNI SNNLPPPLLS NSTGTDFKDE LDEFFKNVST NIPNFGALTQ INTTLLDLSG EMLALQEVVK ALNESYIDLK ELGNY TYYN KWPGSGYIPE APRDGQAYVR KDGEWVLLST FLLEVLFQGP GHHHHHHHHS AWSHPQFEKG GGSGGGGSGG SAWSHP QFE KSA UniProtKB: Spike glycoprotein, Fibritin |
-Macromolecule #3: 2-acetamido-2-deoxy-beta-D-glucopyranose
Macromolecule | Name: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 3 / Number of copies: 33 / Formula: NAG |
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Molecular weight | Theoretical: 221.208 Da |
Chemical component information | ![]() ChemComp-NAG: |
-Macromolecule #4: LINOLEIC ACID
Macromolecule | Name: LINOLEIC ACID / type: ligand / ID: 4 / Number of copies: 3 / Formula: EIC |
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Molecular weight | Theoretical: 280.445 Da |
Chemical component information | ![]() ChemComp-EIC: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TALOS ARCTICA |
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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: 200 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: OTHER / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.8 µm |
Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |