3AVY

Structure of viral RNA polymerase complex 6

Summary for 3AVY

• Entry DOI: 10.2210/pdb3avy/pdb
• Related: 3AVT 3AVU 3AVV 3AVW 3AVX
• Descriptor: Elongation factor Ts, Elongation factor Tu, LINKER, Q beta replicase, RNA (5'-R(*GP*GP*GP*UP*CP*CP*AP*UP*AP*AP*AP*AP*U)-3'), RNA (5'-R(*AP*AP*CP*GP*AP*UP*UP*UP*UP*AP*UP*GP*GP*AP*CP*CP*CP*A)-3'), ... (6 entities in total)
• Functional Keywords: rna polymerase, translation, transferase-rna complex, transferase/rna
• Biological source: Escherichia coli O157:H7; More
• Total number of polymer chains: 3
• Total formula weight: 151848.00

Authors

Takeshita, D.,Tomita, K. (deposition date: 2011-03-08, release date: 2012-01-18, Last modification date: 2023-11-01)

Primary citation

Takeshita, D.,Tomita, K.
Molecular basis for RNA polymerization by Q beta replicase
Nat.Struct.Mol.Biol., 19:229-237, 2012

PubMed Abstract: Core Qβ replicase comprises the Qβ virus-encoded RNA-dependent RNA polymerase (β-subunit) and the host Escherichia coli translational elongation factors EF-Tu and EF-Ts. The functions of the host proteins in the viral replicase are not clear. Structural analyses of RNA polymerization by core Qβ replicase reveal that at the initiation stage, the 3'-adenine of the template RNA provides a stable platform for de novo initiation. EF-Tu in Qβ replicase forms a template exit channel with the β-subunit. At the elongation stages, the C-terminal region of the β-subunit, assisted by EF-Tu, splits the temporarily double-stranded RNA between the template and nascent RNAs before translocation of the single-stranded template RNA into the exit channel. Therefore, EF-Tu in Qβ replicase modulates RNA elongation processes in a distinct manner from its established function in protein synthesis.

PubMed: 22245970
DOI: 10.1038/nsmb.2204

Experimental method

X-RAY DIFFRACTION (2.616 Å)