Zhen Ren and Matthew C. Franklin contributed equally to this work.
Structure of the RNA-directed RNA Polymerase from the cystovirus ϕ12
Article first published online: 1 JUN 2013
Copyright © 2013 Wiley Periodicals, Inc.
Proteins: Structure, Function, and Bioinformatics
Volume 81, Issue 8, pages 1479–1484, August 2013
How to Cite
Ren, Z., Franklin, M. C. and Ghose, R. (2013), Structure of the RNA-directed RNA Polymerase from the cystovirus ϕ12. Proteins, 81: 1479–1484. doi: 10.1002/prot.24297
- Issue published online: 23 JUL 2013
- Article first published online: 1 JUN 2013
- Accepted manuscript online: 9 APR 2013 04:31AM EST
- Manuscript Accepted: 22 MAR 2013
- Manuscript Revised: 9 MAR 2013
- Manuscript Received: 14 FEB 2013
- NSF. Grant Number: MCB 083141
- NIH. Grant Number: 8G12MD007603 (for partial support of CCNY core facilities)
- RNA-directed RNA polymerase;
- de novo initiation;
We have determined the structure of P2, the self-priming RdRp from cystovirus ϕ12 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. Proteins 2013; 81:1479–1484. © 2013 Wiley Periodicals, Inc.