Backbone chemical shift assignments and secondary structure analysis of the U1 protein from the Bas-Congo virus |
| |
Authors: | Garry W. Buchko,Matthew C. Clifton,Ellen G. Wallace,Kateri A. Atkins,Peter J. Myler |
| |
Affiliation: | 1.Seattle Structural Genomics Center for Infectious Disease,Seattle,USA;2.Earth and Biological Sciences Directorate, Pacific Northwest National Laboratory,Richland,USA;3.Beryllium,Bainbridge Island,USA;4.Center for Infectious Disease Research,Seattle,USA;5.Department of Global Health,University of Washington,Seattle,USA;6.Department of Biomedical Informatics and Health Education,University of Washington,Seattle,USA;7.Nurix Inc.,San Francisco,USA |
| |
Abstract: | The Bas-Congo virus (BASV) is the first rhabdovirus associated with a human outbreak of acute hemorrhagic fever. The single-stranded, negative-sense RNA genome of BASV contains the five core genes present in all rhabdoviral genomes plus an additional three genes, annotated U1, U2, and U3, with weak (<21%) sequence similarity only to a handful of genes observed in a few other rhabdoviral genomes. The function of the rhabdoviral U proteins is unknown, but, they are hypothesized to play a role in viral infection or replication. To better understand this unique family of proteins, a construct containing residues 27–203 of the 216-residue U1 protein (BASV-U1*) was prepared. By collecting data in 0.5 M urea it was possible to eliminate transient association enough to enable the assignment of most of the observable 1HN, 1Hα, 15N, 13Cα, 13Cβ, and 13C´ chemical shifts for BASV-U1* that will provide a foundation to study its solution properties. The analyses of these chemical shifts along with 15N-edited NOESY data enabled the identification of the elements of secondary structure present in BASV-U1*. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|