Article
Combined use of residual dipolar couplings and solution X-ray scattering to rapidly probe rigid-body conformational transitions in a non-phosphorylatable active-site mutant of the 128 kDa enzyme I dimer.
Journal of the American Chemical Society - 26 Jan 2011
Takayama Yuki, Schwieters Charles D, Grishaev Alexander, Ghirlando Rodolfo, Clore G Marius
Abstract excerpt
The first component of the bacterial phosphotransferase system, enzyme I (EI), is a multidomain 128 kDa dimer that undergoes large rigid-body conformational transitions during the course of its catalytic cycle. Here we investigate the solution structure of a non-phosphorylatable active-site mutan...
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