2bbp
From Proteopedia
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NMR structures of the peptide linked to the genome (VPg) of poliovirus
Overview
VPgs are essential for replication of picornaviruses, which cause diseases, such as poliomyelitis, foot and mouth disease, and the common cold. VPg in, infected cells is covalently linked to the 5' end of the viral RNA, or, in, a uridylylated form, free in the cytoplasm. We show here the first, solution structure for a picornaviral VPg, that of the 22-residue peptide, from poliovirus serotype 1. VPg in buffer is inherently flexible, but a, single conformer was obtained by adding trimethylamine N-oxide (TMAO)., TMAO had only minor effects on the TOCSY spectrum. However, it increased, the amount of structured peptide, as indicated by more peaks in the NOESY, spectrum and an up to 300% increase in the ratio of normalized NOE cross, peak intensities to that in buffer. The data for VPg in TMAO yielded a, well defined structure bundle with 0.6 A RMSD (versus 6.6 A in buffer, alone), with 10-30 unambiguous constraints per residue. The structure, consists of a large loop region from residues 1 to 14, from which the, reactive tyrosinate projects outward, and a C-terminal helix from residues, 18 to 21 that aligns the sidechains of conserved residues on one face. The, structure has a stable docking position at an area on the poliovirus, polymerase crystal structure identified as a VPg binding site by, mutagenesis studies. Further, UTP and ATP dock in a base-specific manner, to the reactive face of VPg, held in place by residues conserved in all, picornavirus VPgs.
About this Structure
2BBP is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
NMR structure of the viral peptide linked to the genome (VPg) of poliovirus., Schein CH, Oezguen N, Volk DE, Garimella R, Paul A, Braun W, Peptides. 2006 Jul;27(7):1676-84. Epub 2006 Mar 15. PMID:16540201
Page seeded by OCA on Wed Nov 21 08:42:20 2007
