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Yorodumi- EMDB-48153: Cryo-EM structure of SARS-CoV-2 Omicron JN.1.11 spike protein (on... -
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Open data
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Basic information
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| Title | Cryo-EM structure of SARS-CoV-2 Omicron JN.1.11 spike protein (one RBD up state) | |||||||||
Map data | structure of SARS-CoV-2 Omicron JN.1.11 spike protein (one RBD up state) | |||||||||
Sample |
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Keywords | SARS-CoV-2 / COVID-19 / Spike / VIRAL PROTEIN | |||||||||
| Function / homology | Function and homology informationhost cell endoplasmic reticulum-Golgi intermediate compartment membrane / positive regulation of viral entry into host cell / receptor-mediated virion attachment to host cell / host cell surface receptor binding / 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 ...host cell endoplasmic reticulum-Golgi intermediate compartment membrane / positive regulation of viral entry into host cell / receptor-mediated virion attachment to host cell / host cell surface receptor binding / 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 / identical protein binding / membrane Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.93 Å | |||||||||
Authors | Feng Z / Huang J / Ward AB | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: Cell Rep / Year: 2025Title: Structural and functional insights into the evolution of SARS-CoV-2 KP.3.1.1 spike protein. Authors: Ziqi Feng / Jiachen Huang / Sabyasachi Baboo / Jolene K Diedrich / Sandhya Bangaru / James C Paulson / John R Yates / Meng Yuan / Ian A Wilson / Andrew B Ward / ![]() Abstract: The JN.1-sublineage KP.3.1.1 recently emerged as the globally prevalent SARS-CoV-2 variant, demonstrating increased infectivity and antibody escape. We investigate how mutations and a deletion in the ...The JN.1-sublineage KP.3.1.1 recently emerged as the globally prevalent SARS-CoV-2 variant, demonstrating increased infectivity and antibody escape. We investigate how mutations and a deletion in the KP.3.1.1 spike protein (S) affect hACE2 binding and antibody escape. Mass spectrometry confirms a new glycan site at residue N30 that alters the glycoforms at neighboring N61. Cryoelectron microscopy (cryo-EM) structures show that the N30 glycan and rearrangement of adjacent residues do not significantly change the overall spike structure, up-down ratio of receptor-binding domains (RBDs), or hACE2 binding. Furthermore, a KP.3.1.1 S with hACE2 structure further confirms an epistatic effect between F456L and Q493E on hACE2 binding. Our analysis shows that SARS-CoV-2 variants that emerged after late 2023 are now incorporating reversions to residues found in other sarbecoviruses, including the N30 glycan, Q493E, and others. Overall, these results inform on the structural and functional consequences of the KP.3.1.1 mutations, the current SARS-CoV-2 evolutionary trajectory, and immune evasion. | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_48153.map.gz | 484.1 MB | EMDB map data format | |
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| Header (meta data) | emd-48153-v30.xml emd-48153.xml | 19.3 KB 19.3 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_48153_fsc.xml | 17 KB | Display | FSC data file |
| Images | emd_48153.png | 86.2 KB | ||
| Masks | emd_48153_msk_1.map | 512 MB | Mask map | |
| Filedesc metadata | emd-48153.cif.gz | 6.8 KB | ||
| Others | emd_48153_half_map_1.map.gz emd_48153_half_map_2.map.gz | 475.1 MB 475.1 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-48153 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-48153 | HTTPS FTP |
-Validation report
| Summary document | emd_48153_validation.pdf.gz | 1.1 MB | Display | EMDB validaton report |
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| Full document | emd_48153_full_validation.pdf.gz | 1.1 MB | Display | |
| Data in XML | emd_48153_validation.xml.gz | 26.6 KB | Display | |
| Data in CIF | emd_48153_validation.cif.gz | 35 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-48153 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-48153 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9ellMC ![]() 9eleC ![]() 9elfC ![]() 9elgC ![]() 9elhC ![]() 9eliC ![]() 9eljC ![]() 9elkC ![]() 9elmC ![]() 9elnC ![]() 9eloC ![]() 9elpC ![]() 9elqC 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_48153.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | structure of SARS-CoV-2 Omicron JN.1.11 spike protein (one RBD up state) | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.718 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_48153_msk_1.map | ||||||||||||
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| Density Histograms |
-Half map: Half Map B
| File | emd_48153_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_48153_half_map_2.map | ||||||||||||
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| Annotation | Half Map A | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : SARS-CoV-2 Omicron JN.1.11 spike protein
| Entire | Name: SARS-CoV-2 Omicron JN.1.11 spike protein |
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| Components |
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-Supramolecule #1: SARS-CoV-2 Omicron JN.1.11 spike protein
| Supramolecule | Name: SARS-CoV-2 Omicron JN.1.11 spike protein / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Spike glycoprotein
| Macromolecule | Name: Spike glycoprotein / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 133.414234 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: MFVFLVLLPL VSSQCVNLIT TTQSYTNSFT RGVYYPDKVF RSSVLHLTQD LFLPFFSNVT WFHAISGTNG TKRFDNPVLP FNDGVYFAS TEKSNIIRGW IFGTTLDSKT QSLLIVNNAT NVFIKVCEFQ FCNDPFLDVY HKNNKSWMES ESGVYSSANN C TFEYVSQP ...String: MFVFLVLLPL VSSQCVNLIT TTQSYTNSFT RGVYYPDKVF RSSVLHLTQD LFLPFFSNVT WFHAISGTNG TKRFDNPVLP FNDGVYFAS TEKSNIIRGW IFGTTLDSKT QSLLIVNNAT NVFIKVCEFQ FCNDPFLDVY HKNNKSWMES ESGVYSSANN C TFEYVSQP FLMDLEGKQG NFKNLREFVF KNIDGYFKIY SKHTPINIGR DFPQGFSALE PLVDLPIGIN ITRFQTLLAL NR SYLTPGD SSSGWTAGAA DYYVGYLQPR TFLLKYNENG TITDAVDCAL DPLSETKCTL KSFTVEKGIY QTSNFRVQPT ESI VRFPNV TNLCPFHEVF NATRFASVYA WNRTRISNCV ADYSVLYNFA PFFAFKCYGV SPTKLNDLCF TNVYADSFVI KGNE VSQIA PGQTGNIADY NYKLPDDFTG CVIAWNSNKL DSKHSGNYDY WYRSFRKSKL KPFERDISTE IYQAGNKPCK GKGPN CYFP LQSYGFRPTY GVGHQPYRVV VLSFELLHAP ATVCGPKKST NLVKNKCVNF NFNGLTGTGV LTKSNKKFLP FQQFGR DIV DTTDAVRDPQ TLEILDITPC SFGGVSVITP GTNTSNQVAV LYQGVNCTEV SVAIHADQLT PTWRVYSTGS NVFQTRA GC LIGAEYVNNS YECDIPIGAG ICASYQTQTK SRGSASSVAS QSIIAYTMSL GAENSVAYSN NSIAIPTNFT ISVTTEIL P VSMTKTSVDC TMYICGDSTE CSNLLLQYGS FCTQLKRALT GIAVEQDKNT QEVFAQVKQI YKTPPIKYFG GFNFSQILP DPSKPSKRSP IEDLLFNKVT LADAGFIKQY GDCLGDIAAR DLICAQKFNG LTVLPPLLTD EMIAQYTSAL LAGTITSGWT FGAGPALQI PFPMQMAYRF NGIGVTQNVL YENQKLIANQ FNSAIGKIQD SLFSTPSALG KLQDVVNHNA QALNTLVKQL S SKFGAISS VLNDILSRLD PPEAEVQIDR LITGRLQSLQ TYVTQQLIRA AEIRASANLA ATKMSECVLG QSKRVDFCGK GY HLMSFPQ SAPHGVVFLH VTYVPAQEKN FTTAPAICHD GKAHFPREGV FVSNGTHWFL TQRNFYEPQI ITTDNTFVSG NCD VVIGIV NNTVYDPLQL ELDSFKEELD KYFKNHTSPD VDLGDISGIN ASVVNIQKEI DRLNEVAKNL NESLIDLQEL GKYE Q UniProtKB: Spike glycoprotein |
-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: 22 / Formula: NAG |
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| Molecular weight | Theoretical: 221.208 Da |
| Chemical component information | ![]() ChemComp-NAG: |
-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: 7.4 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS GLACIOS |
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| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 44.84 e/Å2 |
| Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.7 µm / Nominal defocus min: 0.7000000000000001 µm |
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Keywords
Authors
United States, 1 items
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Homo sapiens (human)
Processing
FIELD EMISSION GUN

