Minimal nanodisc without exogenous lipids for stabilizing membrane proteins in detergent-free buffer.
Biochim Biophys Acta Biomembr
; 1861(4): 852-860, 2019 04 01.
Article
em En
| MEDLINE
| ID: mdl-30707889
ABSTRACT
Membrane protein stabilization after detergent solubilization presents drawbacks for structural and biophysical studies, in particular that of a reduced stability in detergent micelles. Therefore, alternative methods are required for efficient stabilization. Lipid nanodisc made with the membrane scaffold protein MSP is a valuable system but requires a fine optimization of the lipid to protein ratio. We present here the use of the scaffold protein MSP without added lipids as a minimal system to stabilize membrane proteins. We show that this method is applicable to α-helical and ß-strands transmembrane proteins. This method allowed cryo-electron microscopy structural study of the bacterial transporter MexB. A protein quantification indicates that MexB is stabilized by two MSP proteins. This simplified and efficient method proposes a new advance in harnessing the MSP potential to stabilize membrane proteins.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas da Membrana Bacteriana Externa
/
Nanoestruturas
/
Lipídeos de Membrana
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article