Josts, I, Nitsche, J, Maric, S, Mertens, HD, Moulin, M, Haertlein, M, Prevost, S, Svergun, DI, Busch, S, Forsyth, VT and Tidow, H (2018) Conformational States of ABC Transporter MsbA in a Lipid Environment Investigated by Small-Angle Scattering Using Stealth Carrier Nanodiscs. Structure, 26 (8). 1072 - 1079.e4.

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Abstract

Structural studies of integral membrane proteins (IMPs) are challenging, as many of them are inactive or insoluble in the absence of a lipid environment. Here, we describe an approach making use of fractionally deuterium labeled "stealth carrier" nanodiscs that are effectively invisible to low-resolution neutron diffraction and enable structural studies of IMPs in a lipidic native-like solution environment. We illustrate the potential of the method in a joint small-angle neutron scattering (SANS) and X-ray scattering (SAXS) study of the ATP-binding cassette (ABC) transporter protein MsbA solubilized in the stealth nanodiscs. The data allow for a direct observation of the signal from the solubilized protein without contribution from the surrounding lipid nanodisc. Not only the overall shape but also differences between conformational states of MsbA can be reliably detected from the scattering data, demonstrating the sensitivity of the approach and its general applicability to structural studies of IMPs.

Item Type: Article
Additional Information: The final version of this article is available online at https://www.sciencedirect.com/science/article/pii/S0969212618301710?via%3Dihub
Uncontrolled Keywords: integral membrane proteins; stealth carrier; nanodiscs; macromolecular deuteration; small-angle neutron scattering (SANS)small-angle X-ray scattering (SAXS)ABC transporter; conformational states
Subjects: Q Science > Q Science (General)
Divisions: Faculty of Natural Sciences > School of Life Sciences
Related URLs:
Depositing User: Symplectic
Date Deposited: 05 Feb 2019 16:10
Last Modified: 05 Feb 2019 16:10
URI: http://eprints.keele.ac.uk/id/eprint/5768

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