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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 (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 ?-helices at the dimer interface observed in a crystal structure suggesting this region either undergoes intermediate timescale motion (?s-ms) and/or is heterogeneous.

SUBMITTER: Buchko GW

PROVIDER: S-EPMC4569509 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature

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

Buchko Garry W GW Edwards Thomas E TE Hewitt Stephen N SN Phan Isabelle Q H IQ Van Voorhis Wesley C WC Miller Samuel I SI Myler Peter J PJ

Biomolecular NMR assignments 20150509 2

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 heterogen ...[more]

PMID: 25957069

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