Backbone chemical shift assignments and secondary structure analysis of the U1 protein from the Bas-Congo virus

Buchko, Garry W.; Clifton, Matthew C.; Wallace, Ellen G.; Atkins, Kateri A.; Myler, Peter J.

doi:10.1007/s12104-016-9719-2

Backbone chemical shift assignments and secondary structure analysis of the U1 protein from the Bas-Congo virus

Journal Article · Wed Dec 14 23:00:00 EST 2016 · Biomolecular NMR Assignments

DOI:https://doi.org/10.1007/s12104-016-9719-2· OSTI ID:1339271

Buchko, Garry W. ^[1]; Clifton, Matthew C. ^[2]; Wallace, Ellen G. ^[3]; Atkins, Kateri A. ^[3]; Myler, Peter J. ^[4]

Seattle Structural Genomics Center for Infectious Disease, Seattle, WA (United States); Pacific Northwest National Lab. (PNNL), Richland, WA (United States). Atmospheric Science and Global Change Div. (ASGC)
Seattle Structural Genomics Center for Infectious Disease, Seattle, WA (United States); Beryllium, Bainbridge Island, WA (United States); Nurix Inc., San Francisco, CA (United States)
Seattle Structural Genomics Center for Infectious Disease, Seattle, WA (United States); Beryllium, Bainbridge Island, WA (United States)
Seattle Structural Genomics Center for Infectious Disease, Seattle, WA (United States); Center for Infectious Disease Research, Seattle, WA (United States); Univ. of Washington, Seattle, WA (United States)

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 ¹H^N, ¹Hα, ¹⁵N, ¹³Cα, ¹³Cβ, and ¹³C´ chemical shifts for BASV-U1* that will provide a foundation to study its solution properties. Here, 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*.

Research Organization:: Pacific Northwest National Laboratory (PNNL), Richland, WA (United States)

Sponsoring Organization:: USDOE

Grant/Contract Number:: AC05-76RL01830

OSTI ID:: 1339271

Journal Information:: Biomolecular NMR Assignments, Journal Name: Biomolecular NMR Assignments Journal Issue: 1 Vol. 11; ISSN 1874-2718

Publisher:: SpringerCopyright Statement

Country of Publication:: United States

Language:: English

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Backbone chemical shift assignments and secondary structure analysis of the U1 protein from the Bas-Congo virus

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