5WWP
Crystal structure of Middle East respiratory syndrome coronavirus helicase (MERS-CoV nsp13)
Summary for 5WWP
| Entry DOI | 10.2210/pdb5wwp/pdb |
| Descriptor | ORF1ab, ZINC ION, SULFATE ION (3 entities in total) |
| Functional Keywords | middle east respiratory syndrome coronavirus, nidovirales, coronavirus, mers, nsp13, helicase, sf1 superfamily, atp hydrolysis, atpase, rna 5'-triphosphatase, unwinding, upf1 helicase, arterivirus nsp10, zinc binding domain, ch domain, 1b beta-barrel domain, viral rna synthesis, reca-like domain, cov replication and transcription, hydrolase |
| Biological source | Human betacoronavirus 2c EMC/2012 |
| Cellular location | Host cytoplasm, host perinuclear region . Host membrane ; Multi-pass membrane protein : K0BWD0 |
| Total number of polymer chains | 2 |
| Total formula weight | 133548.54 |
| Authors | Hao, W.,Wojdyla, J.A.,Zhao, R.,Han, R.,Das, R.,Zlatev, I.,Manoharan, M.,Wang, M.,Cui, S. (deposition date: 2017-01-03, release date: 2017-07-05, Last modification date: 2024-10-30) |
| Primary citation | Hao, W.,Wojdyla, J.A.,Zhao, R.,Han, R.,Das, R.,Zlatev, I.,Manoharan, M.,Wang, M.,Cui, S. Crystal structure of Middle East respiratory syndrome coronavirus helicase PLoS Pathog., 13:e1006474-e1006474, 2017 Cited by PubMed Abstract: Middle East respiratory syndrome coronavirus (MERS-CoV) remains a threat to public health worldwide; however, effective vaccine or drug against CoVs remains unavailable. CoV helicase is one of the three evolutionary most conserved proteins in nidoviruses, thus making it an important target for drug development. We report here the first structure of full-length coronavirus helicase, MERS-CoV nsp13. MERS-CoV helicase has multiple domains, including an N-terminal Cys/His rich domain (CH) with three zinc atoms, a beta-barrel domain and a C-terminal SF1 helicase core with two RecA-like subdomains. Our structural analyses show that while the domain organization of nsp13 is conserved throughout nidoviruses, the individual domains of nsp13 are closely related to the equivalent eukaryotic domains of Upf1 helicases. The most distinctive feature differentiating CoV helicases from eukaryotic Upf1 helicases is the interaction between CH domain and helicase core. PubMed: 28651017DOI: 10.1371/journal.ppat.1006474 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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