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Structure and interactions of the RNA-dependent RNA polymerase from bacteriophage phi12 (P1 crystal form)Structure and interactions of the RNA-dependent RNA polymerase from bacteriophage phi12 (P1 crystal form)
Structural highlights
FunctionPublication Abstract from PubMedWe have determined the structure of P2, the self-priming RdRp from cystovirus varphi12 in two crystal forms (A, B) at resolutions of 1.7 A and 2.1 A. 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. (c) 2013 Wiley Periodicals, Inc. Structure of the RNA-directed RNA Polymerase from the cystovirus varphi12.,Ren Z, C Franklin M, Ghose R Proteins. 2013 Aug;81(8):1479-84. doi: 10.1002/prot.24297. Epub 2013 Jun 1. PMID:23568335[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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