4B02

The C-terminal Priming Domain is Strongly Associated with the Main Body of Bacteriophage phi6 RNA-Dependent RNA Polymerase

Summary for 4B02

• Entry DOI: 10.2210/pdb4b02/pdb
• Related: 1HHS 1HHT 1HI0 1HI1 1HI8 1UVI 1UVJ 1UVK 1UVL 1UVM 1UVN 1WAC 2JL9 2JLF 2JLG 4A8F 4A8K 4A8M 4A8O 4A8Q 4A8S 4A8W 4A8Y
• Descriptor: RNA-DIRECTED RNA POLYMERASE, MANGANESE (II) ION (2 entities in total)
• Functional Keywords: viral polymerase, transferase
• Biological source: PSEUDOMONAS PHAGE PHI6
• Cellular location: Virion: P11124
• Total number of polymer chains: 3
• Total formula weight: 224874.42

Authors

Sarin, L.P.,Wright, S.,Chen, Q.,Degerth, L.H.,Stuart, D.I.,Grimes, J.M.,Bamford, D.H.,Poranen, M.M. (deposition date: 2012-06-27, release date: 2012-08-01, Last modification date: 2023-12-20)

Primary citation

Sarin, L.P.,Wright, S.,Chen, Q.,Degerth, L.H.,Stuart, D.I.,Grimes, J.M.,Bamford, D.H.,Poranen, M.M.
The C-Terminal Priming Domain is Strongly Associated with the Main Body of Bacteriophage Phi6 RNA-Dependent RNA Polymerase.
Virology, 432:184-, 2012

PubMed Abstract: Double-stranded RNA viruses encode a single protein species containing RNA-dependent RNA polymerase (RdRP) motifs. This protein is responsible for RNA transcription and replication. The architecture of viral RdRPs resembles that of a cupped right hand with fingers, palm and thumb domains. Those using de novo initiation have a flexible structural elaboration that constitutes the priming platform. Here we investigate the properties of the C-terminal priming domain of bacteriophage ϕ6 to get insights into the role of an extended loop connecting this domain to the main body of the polymerase. Proteolyzed ϕ6 RdRP that possesses a nick in the hinge region of this loop was better suited for de novo initiation. The clipped C-terminus remained associated with the main body of the polymerase via the anchor helix. The structurally flexible hinge region appeared to be involved in the control of priming platform movement. Moreover, we detected abortive initiation products for a bacteriophage RdRP.

PubMed: 22770923
DOI: 10.1016/J.VIROL.2012.05.035

Experimental method

X-RAY DIFFRACTION (3.3 Å)