4B02: The C-Terminal Priming Domain Is Strongly Associated With The Main Body Of Bacteriophage Phi6 Rna-Dependent Rna Polymerase

Citation:
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 varphi6 to get insights into the role of an extended loop connecting this domain to the main body of the polymerase. Proteolyzed varphi6 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.
PDB ID: 4B02Download
MMDB ID: 101645
PDB Deposition Date: 2012/6/27
Updated in MMDB: 2012/08
Experimental Method:
x-ray diffraction
Resolution: 3.3  Å
Source Organism:
Similar Structures:
Biological Unit for 4B02: monomeric; determined by author and by software (PISA)
Molecular Components in 4B02
Label Count Molecule
Protein (1 molecule)
1
RNA-directed RNA Polymerase(Gene symbol: pol)
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

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