5F8L
Enterovirus 71 Polymerase Elongation Complex (C3S1 Form)
Summary for 5F8L
| Entry DOI | 10.2210/pdb5f8l/pdb |
| Related | 5F8G 5F8H 5F8I 5F8J 5F8M 5F8N 5F8O |
| Descriptor | Genome polyprotein, RNA (35-MER), RNA (5'-R(*UP*GP*UP*UP*CP*GP*AP*CP*GP*AP*GP*AP*GP*AP*GP*AP*CP*C)-3'), ... (5 entities in total) |
| Functional Keywords | polymerase-rna complex, elongation, nucleotide addition cycle, transferase-rna complex, transferase/rna |
| Biological source | Enterovirus A71 More |
| Cellular location | Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Virion : E5RPG2 |
| Total number of polymer chains | 3 |
| Total formula weight | 70518.08 |
| Authors | |
| Primary citation | Shu, B.,Gong, P. Structural basis of viral RNA-dependent RNA polymerase catalysis and translocation Proc.Natl.Acad.Sci.USA, 113:E4005-E4014, 2016 Cited by PubMed Abstract: Viral RNA-dependent RNA polymerases (RdRPs) play essential roles in viral genome replication and transcription. We previously reported several structural states of the poliovirus RdRP nucleotide addition cycle (NAC) that revealed a unique palm domain-based active site closure mechanism and proposed a six-state NAC model including a hypothetical state representing translocation intermediates. Using the RdRP from another human enterovirus, enterovirus 71, here we report seven RdRP elongation complex structures derived from a crystal lattice that allows three NAC events. These structures suggested a key order of events in initial NTP binding and NTP-induced active site closure and revealed a bona fide translocation intermediate featuring asymmetric movement of the template-product duplex. Our work provides essential missing links in understanding NTP recognition and translocation mechanisms in viral RdRPs and emphasizes the uniqueness of the viral RdRPs compared with other processive polymerases. PubMed: 27339134DOI: 10.1073/pnas.1602591113 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.812 Å) |
Structure validation
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