[English] 日本語
![](img/lk-miru.gif)
- EMDB-39025: Structure of HCoV-HKU1A spike in the functionally anchored-3up co... -
+
Open data
-
Basic information
Entry | ![]() | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Structure of HCoV-HKU1A spike in the functionally anchored-3up conformation with 3TMPRSS2 | |||||||||
![]() | ||||||||||
![]() |
| |||||||||
![]() | HKU1A / spike / TMPRSS2 / VIRAL PROTEIN | |||||||||
Function / homology | ![]() transmembrane protease serine 2 / protein autoprocessing / Attachment and Entry / serine-type peptidase activity / endocytosis involved in viral entry into host cell / viral translation / Induction of Cell-Cell Fusion / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / Attachment and Entry / positive regulation of viral entry into host cell ...transmembrane protease serine 2 / protein autoprocessing / Attachment and Entry / serine-type peptidase activity / endocytosis involved in viral entry into host cell / viral translation / Induction of Cell-Cell Fusion / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / Attachment and Entry / positive regulation of viral entry into host cell / receptor-mediated virion attachment to host cell / fusion of virus membrane with host plasma membrane / serine-type endopeptidase activity / fusion of virus membrane with host endosome membrane / viral envelope / host cell plasma membrane / virion membrane / proteolysis / extracellular exosome / extracellular region / nucleoplasm / membrane / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.09 Å | |||||||||
![]() | Lu YC / Zhang X / Wang HF / Liu XC / Sun L / Yang HT | |||||||||
Funding support | ![]()
| |||||||||
![]() | ![]() Title: TMPRSS2 and glycan receptors synergistically facilitate coronavirus entry. Authors: Haofeng Wang / Xiaoce Liu / Xiang Zhang / Zhuoqian Zhao / Yuchi Lu / Dingzhe Pu / Zeyang Zhang / Jie Chen / Yajie Wang / Mengfei Li / Xuxue Dong / Yinkai Duan / Yujia He / Qiyu Mao / ...Authors: Haofeng Wang / Xiaoce Liu / Xiang Zhang / Zhuoqian Zhao / Yuchi Lu / Dingzhe Pu / Zeyang Zhang / Jie Chen / Yajie Wang / Mengfei Li / Xuxue Dong / Yinkai Duan / Yujia He / Qiyu Mao / Hangtian Guo / Haoran Sun / Yihan Zhou / Qi Yang / Yan Gao / Xiuna Yang / Hongzhi Cao / Luke Guddat / Lei Sun / Zihe Rao / Haitao Yang / ![]() ![]() Abstract: The entry of coronaviruses is initiated by spike recognition of host cellular receptors, involving proteinaceous and/or glycan receptors. Recently, TMPRSS2 was identified as the proteinaceous ...The entry of coronaviruses is initiated by spike recognition of host cellular receptors, involving proteinaceous and/or glycan receptors. Recently, TMPRSS2 was identified as the proteinaceous receptor for HCoV-HKU1 alongside sialoglycan as a glycan receptor. However, the underlying mechanisms for viral entry remain unknown. Here, we investigated the HCoV-HKU1C spike in the inactive, glycan-activated, and functionally anchored states, revealing that sialoglycan binding induces a conformational change of the NTD and promotes the neighboring RBD of the spike to open for TMPRSS2 recognition, exhibiting a synergistic mechanism for the entry of HCoV-HKU1. The RBD of HCoV-HKU1 features an insertion subdomain that recognizes TMPRSS2 through three previously undiscovered interfaces. Furthermore, structural investigation of HCoV-HKU1A in combination with mutagenesis and binding assays confirms a conserved receptor recognition pattern adopted by HCoV-HKU1. These studies advance our understanding of the complex viral-host interactions during entry, laying the groundwork for developing new therapeutics against coronavirus-associated diseases. | |||||||||
History |
|
-
Structure visualization
Supplemental images |
---|
-
Downloads & links
-EMDB archive
Map data | ![]() | 373 MB | ![]() | |
---|---|---|---|---|
Header (meta data) | ![]() ![]() | 16.8 KB 16.8 KB | Display Display | ![]() |
Images | ![]() | 90.6 KB | ||
Filedesc metadata | ![]() | 6.7 KB | ||
Others | ![]() ![]() | 391.4 MB 391.3 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 663.7 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 663.2 KB | Display | |
Data in XML | ![]() | 18 KB | Display | |
Data in CIF | ![]() | 21.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8y7xMC ![]() 8y7yC ![]() 8y87C ![]() 8y88C ![]() 8y89C ![]() 8y8aC ![]() 8y8bC ![]() 8y8cC ![]() 8y8dC ![]() 8y8eC ![]() 8y8fC ![]() 8y8gC ![]() 8y8hC ![]() 8y8iC ![]() 8y8jC 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: 0.82 Å | ||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
|
-Supplemental data
-Half map: #2
File | emd_39025_half_map_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: #1
File | emd_39025_half_map_2.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-
Sample components
-Entire : HKU1A-TMPRSS2 complex
Entire | Name: HKU1A-TMPRSS2 complex |
---|---|
Components |
|
-Supramolecule #1: HKU1A-TMPRSS2 complex
Supramolecule | Name: HKU1A-TMPRSS2 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
---|---|
Source (natural) | Organism: ![]() |
-Macromolecule #1: Spike glycoprotein
Macromolecule | Name: Spike glycoprotein / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 141.235328 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: VIGDFNCTNF AINDLNTTVP RISEYVVDVS YGLGTYYILD RVYLNTTILF TGYFPKSGAN FRDLSLKGTT YLSTLWYQKP FLSDFNNGI FSRVKNTKLY VNKTLYSEFS TIVIGSVFIN NSYTIVVQPH NGVLEITACQ YTMCEYPHTI CKSKGSSRNE S WHFDKSEP ...String: VIGDFNCTNF AINDLNTTVP RISEYVVDVS YGLGTYYILD RVYLNTTILF TGYFPKSGAN FRDLSLKGTT YLSTLWYQKP FLSDFNNGI FSRVKNTKLY VNKTLYSEFS TIVIGSVFIN NSYTIVVQPH NGVLEITACQ YTMCEYPHTI CKSKGSSRNE S WHFDKSEP LCLFKKNFTY NVSTDWLYFH FYQERGTFYA YYADSGMPTT FLFSLYLGTL LSHYYVLPLT CNAISSNTDN ET LQYWVTP LSKRQYLLKF DNRGVITNAV DCSSSFFSEI QCKTKSLLPN TGVYDLSGFT VKPVATVHRR IPDLPDCDID KWL NNFNVP SPLNWERKIF SNCNFNLSTL LRLVHTDSFS CNNFDESKIY GSCFKSIVLD KFAIPNSRRS DLQLGSSGFL QSSN YKIDT TSSSCQLYYS LPAINVTINN YNPSSWNRRY GFNNFNLSSH SVVYSRYCFS VNNTFCPCAK PSFASSCKSH KPPSA SCPI GTNYRSCEST TVLDHTDWCR CSCLPDPITA YDPRSCSQKK SLVGVGEHCA GFGVDEEKCG VLDGSYNVSC LCSTDA FLG WSYDTCVSNN RCNIFSNFIL NGINSGTTCS NDLLQPNTEV FTDVCVDYDL YGITGQGIFK EVSAVYYNSW QNLLYDS NG NIIGFKDFVT NKTYNIFPCY AGRVSAAFHQ NASSLALLYR NLKCSYVLNN ISLTTQPYFD SYLGCVFNAD NLTDYSVS S CALRMGSGFC VDYNSPSSSS SGGSGSSISA SYRFVTFEPF NVSFVNDSIE SVGGLYEIKI PTNFTIVGQE EFIQTNSPK VTIDCSLFVC SNYAACHDLL SEYGTFCDNI NSILDEVNGL LDTTQLHVAD TLMQGVTLSS NLNTNLHFDV DNINFKSLVG CLGPHCGSS SRSFFEDLLF DKVKLSDVGF VEAYNNCTGG SEIRDLLCVQ SFNGIKVLPP ILSESQISGY TTAATVAAMF P PWSAAAGI PFSLNVQYRI NGLGVTMDVL NKNQKLIATA FNNALLSIQN GFSATNSALA KIQSVVNSNA QALNSLLQQL FN KFGAISS SLQEILSRLD PPEAQVQIDR LINGRLTALN AYVSQQLSDI SLVKFGAALA MEKVNECVKS QSPRINFCGN GNH ILSLVQ NAPYGLLFMH FSYKPISFKT VLVSPGLCIS GDVGIAPKQG YFIKHNDHWM FTGSSYYYPE PISDKNVVFM NTCS VNFTK APLVYLNHSV PKLSDFESEL SHWFKNQTSI APNLTLNLHT INATFLDLYY EMNLIQESIK SLN UniProtKB: Spike glycoprotein |
-Macromolecule #2: Transmembrane protease serine 2
Macromolecule | Name: Transmembrane protease serine 2 / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO / EC number: transmembrane protease serine 2 |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 42.283629 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MGSKCSNSGI ECDSSGTCIN PSNWCDGVSH CPGGEDENRC VRLYGPNFIL QVYSSQRKSW HPVCQDDWNE NYGRAACRDM GYKNNFYSS QGIVDDSGST SFMKLNTSAG NVDIYKKLYH SDACSSKAVV SLRCIACGVN LNDDDDKIVG GESALPGAWP W QVSLHVQN ...String: MGSKCSNSGI ECDSSGTCIN PSNWCDGVSH CPGGEDENRC VRLYGPNFIL QVYSSQRKSW HPVCQDDWNE NYGRAACRDM GYKNNFYSS QGIVDDSGST SFMKLNTSAG NVDIYKKLYH SDACSSKAVV SLRCIACGVN LNDDDDKIVG GESALPGAWP W QVSLHVQN VHVCGGSIIT PEWIVTAAHC VEKPLNNPWH WTAFAGILRQ SFMFYGAGYQ VEKVISHPNY DSKTKNNDIA LM KLQKPLT FNDLVKPVCL PNPGMMLQPE QLCWISGWGA TEEKGKTSEV LNAAKVLLIE TQRCNSRYVY DNLITPAMIC AGF LQGNVD SCQGDSGGPL VTSKNNIWWL IGDTSWGSGC AKAYRPGVYG NVMVFTDWIY RQMRADG UniProtKB: Transmembrane protease serine 2 |
-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: 23 / Formula: NAG |
---|---|
Molecular weight | Theoretical: 221.208 Da |
Chemical component information | ![]() ChemComp-NAG: |
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
![]() | single particle reconstruction |
Aggregation state | particle |
-
Sample preparation
Buffer | pH: 7.5 |
---|---|
Vitrification | Cryogen name: ETHANE |
-
Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.2 µm / Nominal defocus min: 1.2 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
-
Image processing
Startup model | Type of model: NONE |
---|---|
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.09 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 935674 |
Initial angle assignment | Type: PROJECTION MATCHING |
Final angle assignment | Type: PROJECTION MATCHING |