Proton-detected solid-state NMR spectroscopy of a zinc diffusion facilitator protein in native nanodiscs

Beate Bersch (1) , Jonas M Dörr (2) , Audrey Hessel (1) , J. Antoinette Killian (2) , Paul Schanda (1, 2)

1 IBS - UMR 5075 - Institut de biologie structurale
2 Universiteit Utrecht / Utrecht University [Utrecht]

The structure, dynamics and function of membrane proteins are intimately linked to the properties of the membrane environment in which the proteins are embedded. For structural and biophysical characterization, membrane proteins generally need to be extracted from the membrane, and reconstituted in a suitable membrane-mimicking environment. Ensuring functional and structural integrity in these environments is often a major concern. The styrene/maleic acid co-polymer has recently been shown to be able to extract lipid/membrane protein patches directly from native membranes, forming nanosize discoidal proteolipid particles, also referred to as native nanodiscs. Here we show, for the first time, that high-resolution solid-state NMR spectra can be obtained from an integral membrane protein in native nanodiscs, as exemplified with the 2 x 34 kDa-large bacterial cation diffusion facilitator CzcD from Cupriavidus metallidurans CH34.

Mots clés: nanodiscs; copolymers; membrane proteins; NMR spectroscopy; solid-state NMR

Domaines: Chimie; Biologie structurale [q-bio.BM]

Beate Bersch, Jonas M Dörr, Audrey Hessel, J. Antoinette Killian, Paul Schanda. Proton-detected solid-state NMR spectroscopy of a zinc diffusion facilitator protein in native nanodiscs. Angewandte Chemie International Edition, 2017, 56 (9), pp.2508-2512. ⟨10.1002/anie.201610441⟩. ⟨hal-01433745⟩