5wwp | pdb_00005wwp

Crystal structure of Middle East respiratory syndrome coronavirus helicase (MERS-CoV nsp13)

spinqualitylabelsall models 5wwp, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5wwp is a 2 chain structure with sequence from Human betacoronavirus 2c EMC/2012. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3Å Ligands: SO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function K0BWD0_MERS Publication Abstract from PubMed 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. Crystal structure of Middle East respiratory syndrome coronavirus helicase.,Hao W, Wojdyla JA, Zhao R, Han R, Das R, Zlatev I, Manoharan M, Wang M, Cui S PLoS Pathog. 2017 Jun 26;13(6):e1006474. doi: 10.1371/journal.ppat.1006474., eCollection 2017 Jun. PMID:28651017 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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