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PEP-19 modulates calcium binding to calmodulin by electrostatic steering.

Xu Wang1, John A Putkey1

  • 1Department of Biochemistry and Molecular Biology, McGovern Medical at UTHealth, 6431 Fannin, Houston, Texas 77030, USA.

Nature Communications
|November 24, 2016
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Summary

PEP-19 protein enhances calcium binding to calmodulin (CaM) through a novel mechanism. Its acidic sequence interacts with CaM, electrostatically guiding calcium ions to binding sites.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Cell Biology

Background:

  • Calmodulin (CaM) is a crucial calcium-binding protein involved in cellular signaling.
  • PEP-19 is a small protein known to modulate CaM's calcium-binding rates.
  • The precise mechanism by which PEP-19 affects CaM's calcium affinity remains unclear.

Purpose of the Study:

  • To elucidate the structural basis of the interaction between PEP-19 and the C-domain of apo calmodulin (CaM).
  • To understand the mechanism by which PEP-19 enhances calcium ion (Ca2+) binding to CaM.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy was used to determine the solution structure of the PEP-19/CaM C-domain complex.
  • Analysis of protein-protein interactions and electrostatic surface potentials.

Main Results:

  • The NMR structure reveals that PEP-19's acidic sequence binds to the interhelical region (between helices E and F) of CaM via hydrophobic interactions.
  • This interaction creates a negatively charged surface on PEP-19, resembling a 'catcher's mitt', positioned near Ca2+ binding loop III of CaM.
  • The structural and electrostatic features suggest a mechanism for accelerated Ca2+ uptake.

Conclusions:

  • PEP-19 enhances Ca2+ binding rates to CaM's C-domain by electrostatically 'catching' and steering Ca2+ ions to the binding site.
  • This mechanism explains how PEP-19 sensitizes cells to calcium signaling events, such as ATP-induced Ca2+ release.
  • The findings provide critical insights into the regulation of CaM-mediated cellular processes.