Computational design and molecular dynamics simulations suggest the mode of substrate binding in ceramide synthases

Iris D. Zelnik, Beatriz Mestre, Jonathan J. Weinstein, Tamir Dingjan, Stav Izrailov, Shifra Ben-Dor, Sarel J. Fleishman and Anthony H. Futerman ()
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Iris D. Zelnik: Weizmann Institute of Science
Beatriz Mestre: Weizmann Institute of Science
Jonathan J. Weinstein: Weizmann Institute of Science
Tamir Dingjan: Weizmann Institute of Science
Stav Izrailov: Weizmann Institute of Science
Shifra Ben-Dor: Weizmann Institute of Science
Sarel J. Fleishman: Weizmann Institute of Science
Anthony H. Futerman: Weizmann Institute of Science

Nature Communications, 2023, vol. 14, issue 1, 1-6

Abstract: Abstract Until now, membrane-protein stabilization has relied on iterations of mutations and screening. We now validate a one-step algorithm, mPROSS, for stabilizing membrane proteins directly from an AlphaFold2 model structure. Applied to the lipid-generating enzyme, ceramide synthase, 37 designed mutations lead to a more stable form of human CerS2. Together with molecular dynamics simulations, we propose a pathway by which substrates might be delivered to the ceramide synthases.

Date: 2023
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DOI: 10.1038/s41467-023-38047-x

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