4N0N
Crystal structure of Arterivirus nonstructural protein 10 (helicase)
Summary for 4N0N
| Entry DOI | 10.2210/pdb4n0n/pdb |
| Related | 4N0O |
| Descriptor | Replicase polyprotein 1ab, ZINC ION, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | arterivirus, helicase, zbd, nsp10, hydrolase |
| Biological source | Equine arteritis virus (EAV) |
| Cellular location | Nsp1 papain-like cysteine proteinase: Host nucleus. Nsp2 cysteine proteinase: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 3: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 5-6-7: Host membrane; Multi-pass membrane protein (Potential). 3C-like serine proteinase: Host cytoplasm (Potential). RNA-directed RNA polymerase: Host cytoplasm, host perinuclear region (Potential). Helicase: Host cytoplasm, host perinuclear region (Potential): P19811 |
| Total number of polymer chains | 1 |
| Total formula weight | 46356.23 |
| Authors | |
| Primary citation | Deng, Z.,Lehmann, K.C.,Li, X.,Feng, C.,Wang, G.,Zhang, Q.,Qi, X.,Yu, L.,Zhang, X.,Feng, W.,Wu, W.,Gong, P.,Tao, Y.,Posthuma, C.C.,Snijder, E.J.,Gorbalenya, A.E.,Chen, Z. Structural basis for the regulatory function of a complex zinc-binding domain in a replicative arterivirus helicase resembling a nonsense-mediated mRNA decay helicase. Nucleic Acids Res., 42:3464-3477, 2014 Cited by PubMed Abstract: All positive-stranded RNA viruses with genomes>∼7 kb encode helicases, which generally are poorly characterized. The core of the nidovirus superfamily 1 helicase (HEL1) is associated with a unique N-terminal zinc-binding domain (ZBD) that was previously implicated in helicase regulation, genome replication and subgenomic mRNA synthesis. The high-resolution structure of the arterivirus helicase (nsp10), alone and in complex with a polynucleotide substrate, now provides first insights into the structural basis for nidovirus helicase function. A previously uncharacterized domain 1B connects HEL1 domains 1A and 2A to a long linker of ZBD, which further consists of a novel RING-like module and treble-clef zinc finger, together coordinating three Zn atoms. On substrate binding, major conformational changes were evident outside the HEL1 domains, notably in domain 1B. Structural characterization, mutagenesis and biochemistry revealed that helicase activity depends on the extensive relay of interactions between the ZBD and HEL1 domains. The arterivirus helicase structurally resembles the cellular Upf1 helicase, suggesting that nidoviruses may also use their helicases for post-transcriptional quality control of their large RNA genomes. PubMed: 24369429DOI: 10.1093/nar/gkt1310 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
Download full validation report
