3pmk
Crystal structure of the Vesicular Stomatitis Virus RNA free nucleoprotein/phosphoprotein complexCrystal structure of the Vesicular Stomatitis Virus RNA free nucleoprotein/phosphoprotein complex
Structural highlights
FunctionPublication Abstract from PubMedReplication of non-segmented negative-strand RNA viruses requires the continuous supply of the nucleoprotein (N) in the form of a complex with the phosphoprotein (P). Here, we present the structural characterization of a soluble, heterodimeric complex between a variant of vesicular stomatitis virus N lacking its 21 N-terminal residues (N(Delta21)) and a peptide of 60 amino acids (P(60)) encompassing the molecular recognition element (MoRE) of P that binds RNA-free N (N(0)). The complex crystallized in a decameric circular form, which was solved at 3.0 A resolution, reveals how the MoRE folds upon binding to N and competes with RNA binding and N polymerization. Small-angle X-ray scattering experiment and NMR spectroscopy on the soluble complex confirms the binding of the MoRE and indicates that its flanking regions remain flexible in the complex. The structure of this complex also suggests a mechanism for the initiation of viral RNA synthesis. Structure of the vesicular stomatitis virus N-P complex.,Leyrat C, Yabukarski F, Tarbouriech N, Ribeiro EA Jr, Jensen MR, Blackledge M, Ruigrok RW, Jamin M PLoS Pathog. 2011 Sep;7(9):e1002248. Epub 2011 Sep 22. PMID:21960769[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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