Phosphorylation of serine-46 in HPr, a key regulatory protein in bacteria, results in stabilization of its solution structure

Protein Science : a Publication of the Protein Society
K PullenR E Klevit

Abstract

The serine-phosphorylated form of histidine-containing protein (HPr), a component of the phosphoenolpyruvate:sugar phosphotransferase system from Bacillus subtilis, has been characterized by NMR spectroscopy and solvent denaturation studies. The results indicate that phosphorylation of Ser 46, the N-cap of alpha-helix-B, does not cause a conformational change but rather stabilizes the helix. Amide proton exchange rates in helix-B are decreased and phosphorylation stabilizes the protein to solvent and thermal denaturation, with a delta delta G of 0.7-0.8 kcal mol-1. A mutant in which Ser 46 is replaced by aspartic acid shows a similar stabilization, indicating that an electrostatic interaction between the negatively charged groups and the helix macrodipole contributes significantly to the stabilization.

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Citations

Feb 17, 1999·Biopolymers·J L Smart, J A McCammon
Oct 23, 1997·Protein Science : a Publication of the Protein Society·B E JonesR E Klevit
Jan 22, 1998·Current Opinion in Structural Biology·M M McEvoy, F W Dahlquist
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Sep 19, 2009·Biochimica Et Biophysica Acta·Peter TerieteFrancesca M Marassi
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Aug 20, 2002·The Journal of Biological Chemistry·Frederico Faria MirandaAurora Martínez
Jun 30, 2019·Journal of Biomolecular Structure & Dynamics·Likun ZhaoZhuqing Zhang
Feb 1, 1996·Microbiology·Milton H SaierJing-Jing Ye
May 21, 2021·EMBO Reports·Elyse S FischerDavid Barford

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