PEP-19 modulates calcium binding to calmodulin by electrostatic steering

Xu Wang and John A. Putkey ()
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Xu Wang: McGovern Medical at UTHealth, 6431 Fannin
John A. Putkey: McGovern Medical at UTHealth, 6431 Fannin

Nature Communications, 2016, vol. 7, issue 1, 1-10

Abstract: Abstract PEP-19 is a small protein that increases the rates of Ca2+ binding to the C-domain of calmodulin (CaM) by an unknown mechanism. Although an IQ motif promotes binding to CaM, an acidic sequence in PEP-19 is required to modulate Ca2+ binding and to sensitize HeLa cells to ATP-induced Ca2+ release. Here, we report the NMR solution structure of a complex between PEP-19 and the C-domain of apo CaM. The acidic sequence of PEP-19 associates between helices E and F of CaM via hydrophobic interactions. This allows the acidic side chains in PEP-19 to extend toward the solvent and form a negatively charged surface that resembles a catcher’s mitt near Ca2+ binding loop III of CaM. The topology and gradients of negative electrostatic surface potential support a mechanism by which PEP-19 increases the rate of Ca2+ binding to the C-domain of CaM by ‘catching’ and electrostatically steering Ca2+ to site III.

Date: 2016
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DOI: 10.1038/ncomms13583

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