Solution structure of gp17 from the Siphoviridae bacteriophage SPP1: Insights into its role in virion assembly
Version of Record online: 9 NOV 2011
Copyright © 2011 Wiley Periodicals, Inc.
Proteins: Structure, Function, and Bioinformatics
Volume 80, Issue 1, pages 319–326, January 2012
How to Cite
Chagot, B., Auzat, I., Gallopin, M., Petitpas, I., Gilquin, B., Tavares, P. and Zinn-Justin, S. (2012), Solution structure of gp17 from the Siphoviridae bacteriophage SPP1: Insights into its role in virion assembly. Proteins, 80: 319–326. doi: 10.1002/prot.23191
- Issue online: 13 DEC 2011
- Version of Record online: 9 NOV 2011
- Accepted manuscript online: 15 SEP 2011 05:17AM EST
- Manuscript Accepted: 7 SEP 2011
- Manuscript Revised: 2 SEP 2011
- Manuscript Received: 7 JUL 2011
- Agence Nationale de la Recherche. Grant Number: ANR-09-BLAN-0149-01 “DNA Gating”
- Commissariat à l'Energie Atomique
- Centre National de la Recherche Scientifique
Additional Supporting Information may be found in the online version of this article.
|PROT_23191_sm_suppinfofig1.tif||1910K||Supporting Information Figure S1: Backbone dynamics of gp17. (A) 15N longitudinal relaxation rates R1, (B) 15N transverse relaxation rates R2 and (C) 1H15N NOEs are plotted as a function of the sequence.|
|PROT_23191_sm_suppinfofig2.tif||5427K||Supporting Information Figure S2: Amino acid sequence conservation within the gp17 (top) and gpU (bottom) protein families. Sequence alignments of gp17 and gpU with 10 homolog representatives (identified by their GI numbers) are shown. Conserved buried residues are boxed in green and conserved solvent exposed residues are boxed in orange. Secondary structure representations of gp17 NMR solution structure and gpU NMR and X-ray structures are plotted. Secondary structures elements are labeled; α-helices are colored in red and β-sheets in blue.|
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