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4A8M

Non-Catalytic Ions Direct the RNA-Dependent RNA Polymerase of Bacterial dsRNA virus phi6 from De Novo Initiation to Elongation

Summary for 4A8M
Entry DOI10.2210/pdb4a8m/pdb
Related1HHS 1HHT 1HI0 1HI1 1HI8 1UVI 1UVJ 1UVK 1UVL 1UVM 1UVN 1WAC 2JL9 2JLF 2JLG 4A8F 4A8K 4A8O 4A8Q 4A8S 4A8W
Descriptor5'-D(*AP*AP*TP*CP)-3', RNA-DIRECTED RNA POLYMERASE, MAGNESIUM ION, ... (5 entities in total)
Functional Keywordstransferase-dna complex, viral polymerase, transferase/dna
Biological sourcePSEUDOMONAS PHAGE PHI6
More
Cellular locationVirion: P11124
Total number of polymer chains4
Total formula weight229442.02
Authors
Wright, S.,Poranen, M.M.,Bamford, D.H.,Stuart, D.I.,Grimes, J.M. (deposition date: 2011-11-21, release date: 2012-07-04, Last modification date: 2024-05-08)
Primary citationWright, S.,Poranen, M.M.,Bamford, D.H.,Stuart, D.I.,Grimes, J.M.
Noncatalytic Ions Direct the RNA-Dependent RNA Polymerase of Bacterial Double-Stranded RNA Virus Phi6 from De Novo Initiation to Elongation.
J.Virol., 86:2837-, 2012
Cited by
PubMed Abstract: RNA-dependent RNA polymerases (RdRps) are key to the replication of RNA viruses. A common divalent cation binding site, distinct from the positions of catalytic ions, has been identified in many viral RdRps. We have applied biochemical, biophysical, and structural approaches to show how the RdRp from bacteriophage ϕ6 uses the bound noncatalytic Mn(2+) to facilitate the displacement of the C-terminal domain during the transition from initiation to elongation. We find that this displacement releases the noncatalytic Mn(2+), which must be replaced for elongation to occur. By inserting a dysfunctional Mg(2+) at this site, we captured two nucleoside triphosphates within the active site in the absence of Watson-Crick base pairing with template and mapped movements of divalent cations during preinitiation. These structures refine the pathway from preinitiation through initiation to elongation for the RNA-dependent RNA polymerization reaction, explain the role of the noncatalytic divalent cation in 6 RdRp, and pinpoint the previously unresolved Mn(2+)-dependent step in replication.
PubMed: 22205747
DOI: 10.1128/JVI.05168-11
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.92 Å)
Structure validation

227933

数据于2024-11-27公开中

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