6MWM
Bat coronavirus HKU4 SUD-C
Summary for 6MWM
| Entry DOI | 10.2210/pdb6mwm/pdb |
| NMR Information | BMRB: 30531 |
| Descriptor | Non-structural protein 3 (1 entity in total) |
| Functional Keywords | coronavirus, viral protein |
| Biological source | Bat coronavirus HKU4 (BtCoV) |
| Total number of polymer chains | 1 |
| Total formula weight | 9122.30 |
| Authors | Staup, A.J.,De Silva, I.U.,Catt, J.T.,Tan, X.,Hammond, R.G.,Johnson, M.A. (deposition date: 2018-10-29, release date: 2019-09-11, Last modification date: 2024-05-15) |
| Primary citation | Staup, A.J.,De Silva, I.U.,Catt, J.T.,Tan, X.,Hammond, R.G.,Johnson, M.A. Structure of the SARS-Unique Domain C From the Bat Coronavirus HKU4. Nat Prod Commun, 14:1934578X19849202-1934578X19849202, 2019 Cited by PubMed Abstract: Coronaviruses (CoVs) that cause infections such as severe acute respiratory syndrome (SARS) and Middle East respiratory syndrome phylogenetically originate from bat CoVs. The coronaviral nonstructural protein 3 (nsp3) has been implicated in viral replication, polyprotein cleavage, and host immune interference. We report the structure of the C domain from the SARS-Unique Domain of bat CoV HKU4. The protein has a frataxin fold, consisting of 5 antiparallel β strands packed against 2 α helices. Bioinformatics analyses and nuclear magnetic resonance experiments were conducted to investigate the function of HKU4 C. The results showed that HKU4 C engages in protein-protein interactions with the nearby M domain of nsp3. The HKU4 C residues involved in protein-protein interactions are conserved in group 2c CoVs, indicating a conserved function. PubMed: 32395093DOI: 10.1177/1934578X19849202 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
