5XGR
Structure of the S1 subunit C-terminal domain from bat-derived coronavirus HKU5 spike protein
Summary for 5XGR
| Entry DOI | 10.2210/pdb5xgr/pdb |
| Descriptor | Spike protein S1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | mers-cov, batcov hku5, ctd, evolution, viral protein |
| Biological source | Bat coronavirus HKU5 (BtCoV) |
| Cellular location | Spike protein S2: Virion membrane ; Single-pass type I membrane protein . Spike protein S1: Virion membrane ; Peripheral membrane protein : A3EXD0 |
| Total number of polymer chains | 8 |
| Total formula weight | 186540.73 |
| Authors | |
| Primary citation | Han, X.,Qi, J.,Song, H.,Wang, Q.,Zhang, Y.,Wu, Y.,Lu, G.,Yuen, K.Y.,Shi, Y.,Gao, G.F. Structure of the S1 subunit C-terminal domain from bat-derived coronavirus HKU5 spike protein Virology, 507:101-109, 2017 Cited by PubMed Abstract: Accumulating evidence indicates that MERS-CoV originated from bat coronaviruses (BatCoVs). Previously, we demonstrated that both MERS-CoV and BatCoV HKU4 use CD26 as a receptor, but how the BatCoVs evolved to bind CD26 is an intriguing question. Here, we solved the crystal structure of the S1 subunit C-terminal domain of HKU5 (HKU5-CTD), another BatCoV that is phylogenetically related to MERS-CoV but cannot bind to CD26. We observed that the conserved core subdomain and those of other betacoronaviruses (betaCoVs) have a similar topology of the external subdomain, indicating the same ancestor of lineage C betaCoVs. However, two deletions in two respective loops located in HKU5-CTD result in conformational variations in CD26-binding interface and are responsible for the non-binding of HKU5-CTD to CD26. Combined with sequence variation in the HKU5-CTD receptor binding interface, we propose the necessity for surveilling the mutation in BatCoV HKU5 spike protein in case of bat-to-human interspecies transmission. PubMed: 28432925DOI: 10.1016/j.virol.2017.04.016 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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