4a8f | pdb_00004a8f

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

spinqualitylabelsall models 4a8f, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4a8f is a 4 chain structure with sequence from Pseudomonas phage phi6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ATP, MG Related: 2jlg, 1uvn, 1uvj, 1hht, 2jl9, 2jlf, 1hi1, 1wac, 1uvm, 4a8k, 1uvk, 1hhs, 1hi0, 1uvi, 1uvl, 1hi8, 4a8m, 4a8o, 4a8q, 4a8w, 4a8s, 4a8y Activity: RNA-directed RNA polymerase, with EC number 2.7.7.48 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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 varphi6 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. Noncatalytic ions direct the RNA-dependent RNA polymerase of bacterial double-stranded RNA virus varphi6 from de novo initiation to elongation.,Wright S, Poranen MM, Bamford DH, Stuart DI, Grimes JM J Virol. 2012 Mar;86(5):2837-49. Epub 2011 Dec 28. PMID:22205747 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also RNA polymerase

Proteopedia Page Contributors and Editors (what is this?)

OCA