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Backbone resonance assignment of the response regulator protein PhoB NF20D from Escherichia coli
KOU 1.2, Xinhui - Personal Name

hoB N is dimerized in both situations. However, we have found that the apo form of P hoB N has multiple confor-mational changes in solution that is hard to be distinguished by using NMR spectroscopy, while the mutagenesis of F20D PhoB N gives homogeneous dispersed signals in HSQC spectrum indicating a relatively uniform conformation. Meanwhile the F20D mutant has the same phosphorylation activity as the wild type protein. Here we report the backbone assignment of PhoB NF20D mutant. The chemical shift (HN, N, CO, C α and C β ) analysis shows that the predicted regions of secondary structure are in good agreement with those observed in the crystal structure of apo PhoB N . Therefore, the backbone chemical shifts assignment of PhoB NF20D mutant would be useful for studying the structure and dynamics of PhoB receiver domain
and it has significance for explaining the mechanism of phosphorylation in TCSs.
EB00000003109K | Available |
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Statement of Responsibility
Xinhui Kou 1.2