2bbp
From Proteopedia
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[[Image:2bbp.gif|left|200px]] | [[Image:2bbp.gif|left|200px]] | ||
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'''NMR structures of the peptide linked to the genome (VPg) of poliovirus''' | '''NMR structures of the peptide linked to the genome (VPg) of poliovirus''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BBP is a [[Single protein]] structure | + | 2BBP is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BBP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Oezguen, N.]] | [[Category: Oezguen, N.]] | ||
[[Category: Schein, C H.]] | [[Category: Schein, C H.]] | ||
| - | [[Category: | + | [[Category: Flexible structure]] |
| - | [[Category: | + | [[Category: Picornavirus]] |
| - | [[Category: | + | [[Category: Rna transcription primer]] |
| - | [[Category: | + | [[Category: Viral polymerase]] |
| - | [[Category: | + | [[Category: Vpg]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:04:57 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 17:05, 3 May 2008
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. 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 Sat May 3 20:04:57 2008
