1UVN: The structural basis for RNA specificity and Ca2 inhibition of an RNA-dependent RNA polymerase phi6p2 ca2+ inhibition complex

The RNA-dependent RNA polymerase of bacteriophage phi6 transcribes mRNA from the three segments of the dsRNA viral genome. We have cocrystallized RNA oligonucleotides with the polymerase, revealing the mode of binding of RNA templates. This binding is somewhat different from that previously seen for DNA oligomers, leading to additional RNA-protein hydrogen bonds, consistent with a preference for RNA. Activation of the RNA/polymerase complex by the addition of substrate and Mg2+ initiates a single round of reaction within the crystal to form a dead-end complex that partially collapses within the enzyme active site. By replacing Mg2+ with Ca2+, we have been able to capture the inhibited complex which shows distortion that explains the structural basis for the inhibition of such polymerases by Ca2+.
PDB ID: 1UVNDownload
MMDB ID: 51734
PDB Deposition Date: 2004/1/21
Updated in MMDB: 2012/10
Experimental Method:
x-ray diffraction
Resolution: 3  Å
Source Organism:
Pseudomonas virus phi6
Similar Structures:
Biological Unit for 1UVN: dimeric; determined by author and by software (PQS)
Molecular Components in 1UVN
Label Count Molecule
Proteins (2 molecules)
RNA-directed RNA Polymerase(Gene symbol: pol)
Molecule annotation
Nucleotide(1 molecule)
Molecule annotation
Chemicals (5 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB