1WAC

Back-priming mode of Phi6 RNA-dependent RNA polymerase

Summary for 1WAC

• Entry DOI: 10.2210/pdb1wac/pdb
• Related: 1HHS 1HHT 1HI0 1HI1 1HI8 1UVI 1UVJ 1UVK 1UVL 1UVM 1UVN
• Descriptor: P2 PROTEIN (1 entity in total)
• Functional Keywords: polymerase, phi6 rna-dependent rna polymerase, transcription
• Biological source: PSEUDOMONAS PHAGE PHI-6
• Cellular location: Virion: P11124
• Total number of polymer chains: 3
• Total formula weight: 223321.94

Authors

Laurila, M.R.L.,Salgado, P.S.,Stuart, D.I.,Grimes, J.M.,Bamford, D.H. (deposition date: 2004-10-26, release date: 2005-01-27, Last modification date: 2023-12-13)

Primary citation

Laurila, M.R.L.,Salgado, P.S.,Stuart, D.I.,Grimes, J.M.,Bamford, D.H.
Back-Priming Mode of Phi6 RNA-Dependent RNA Polymerase
J.Gen.Virol., 86:521-, 2005

PubMed Abstract: The RNA-dependent RNA polymerase of the double-stranded RNA bacteriophage phi6 is capable of primer-independent initiation, as are many RNA polymerases. The structure of this polymerase revealed an initiation platform, composed of a loop in the C-terminal domain (QYKW, aa 629-632), that was essential for de novo initiation. A similar element has been identified in hepatitis C virus RNA-dependent RNA polymerase. Biochemical studies have addressed the role of this platform, revealing that a mutant version can utilize a back-priming initiation mechanism, where the 3' terminus of the template adopts a hairpin-like conformation. Here, the mechanism of back-primed initiation is studied further by biochemical and structural methods.

PubMed: 15659773
DOI: 10.1099/VIR.0.80492-0

Experimental method

X-RAY DIFFRACTION (3 Å)