Structure of the RNA‐directed RNA Polymerase from the cystovirus ϕ12 | Zendy

Ren Zhen | Zendy; Franklin Matthew C. | Zendy; Ghose Ranajeet | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Premium

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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research