Backbone chemical shift assignments for the sensor domain of the Burkholderia pseudomallei histidine kinase RisS – "missing" resonances at the dimer interface | Journal Article

September 17, 2015

Journal Article

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

Abstract

Using a deuterated sample, all the observable backbone 1HN, 15N, 13Ca, and 13C´ 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 1H-15N HSQC spectrum and map primarily onto a-helices at the dimer interface observed in a crystal structure suggesting this region either undergoes intermediate timescale motion (µs – ms) and/or is heterogeneous.

Revised: September 28, 2015 | Published: September 17, 2015

Citation

Buchko G.W., T.E. Edwards, S.N. Hewitt, I. Phan, W.C. Van Voorhis, S.I. Miller, and P.J. Myler. 2015. Backbone chemical shift assignments for the sensor domain of the Burkholderia pseudomallei histidine kinase RisS – "missing resonances at the dimer interface." Biomolecular NMR Assignments 9, no. 2:381-385. PNWD-SA-10406. doi:10.1007/s12104-015-9614-2