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Biomol NMR Assign. 2015 Oct;9(2):381-5. doi: 10.1007/s12104-015-9614-2. Epub 2015 May 9.

Backbone chemical shift assignments for the sensor domain of the Burkholderia pseudomallei histidine kinase RisS: "missing" resonances at the dimer interface.

Author information

1
Seattle Structural Genomics Center for Infectious Disease, Seattle, USA. garry.buchko@pnnl.gov.
2
Biological Sciences Division, Pacific Northwest National Laboratory, Richland, WA, 99352, USA. garry.buchko@pnnl.gov.
3
Seattle Structural Genomics Center for Infectious Disease, Seattle, USA.
4
Beryllium, Bainbridge Island, WA, 98110, USA.
5
Department of Medicine, University of Washington, Seattle, WA, 98195-7185, USA.
6
Center for Infectous Disease Research, formerly Seattle Biomedical Research Institute, Seattle, WA, 98109-5219, USA.
7
Department of Microbiology and Department of Genome Sciences, University of Washington, Seattle, WA, 98195, USA.
8
Department of Biomedical Informatics and Medical Education and Department of Global Health, University of Washington, Seattle, WA, 98195, USA.

Abstract

Using a deuterated sample, all the observable backbone (1)H(N), (15)N, (13)C(a), and (13)C' chemical shifts for the dimeric, periplasmic sensor domain of the Burkholderia pseudomallei histidine kinase RisS were assigned. Approximately one-fifth of the amide resonances are "missing" in the (1)H-(15)N HSQC spectrum and map primarily onto α-helices at the dimer interface observed in a crystal structure suggesting this region either undergoes intermediate timescale motion (μs-ms) and/or is heterogeneous.

KEYWORDS:

Chemical shift perturbations; Infectious diseases; Meliodosis; Signal transduction; Two-component system

PMID:
25957069
PMCID:
PMC4569509
DOI:
10.1007/s12104-015-9614-2
[Indexed for MEDLINE]
Free PMC Article

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