Abstract
We have determined the structure of P2, the self-priming RdRp from cystovirus φ{symbol}12 in two crystal forms (A, B) at resolutions of 1.7 Å and 2.1 Å. Form A contains Mg2+ bound at a site that deviates from the canonical noncatalytic position seen in form B. These structures provide insight into the temperature sensitivity of a ts-mutant. However, the tunnel through which template ssRNA accesses the active site is partially occluded by a flexible loop; this feature, along with suboptimal positioning of other structural elements that prevent the formation of a stable initiation complex, indicate an inactive conformation in crystallo.
Original language | English |
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Pages (from-to) | 1479-1484 |
Number of pages | 6 |
Journal | Proteins: Structure, Function and Bioinformatics |
Volume | 81 |
Issue number | 8 |
DOIs | |
State | Published - Aug 2013 |
Keywords
- Bacteriophage
- Cystovirus
- RNA-directed RNA polymerase
- Replication
- Transcription
- de novo initiation