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Structure of the RNA‐directed RNA Polymerase from the cystovirus ϕ12
Author(s) -
Ren Zhen,
Franklin Matthew C.,
Ghose Ranajeet
Publication year - 2013
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24297
Subject(s) - rna , chemistry , crystal structure , mutant , priming (agriculture) , crystallography , rna polymerase , loop (graph theory) , physics , stereochemistry , biology , biochemistry , gene , mathematics , combinatorics , botany , germination
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 Mg 2+ 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.