Structure of the RNA-directed RNA Polymerase from the cystovirus ϕ12

Zhen Ren, Matthew C. Franklin, Ranajeet Ghose

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

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 languageEnglish
Pages (from-to)1479-1484
Number of pages6
JournalProteins: Structure, Function and Bioinformatics
Volume81
Issue number8
DOIs
StatePublished - Aug 2013

Keywords

  • Bacteriophage
  • Cystovirus
  • RNA-directed RNA polymerase
  • Replication
  • Transcription
  • de novo initiation

Fingerprint

Dive into the research topics of 'Structure of the RNA-directed RNA Polymerase from the cystovirus ϕ12'. Together they form a unique fingerprint.

Cite this