Two-state folding of the outer membrane protein X into a lipid bilayer membrane

Rath, Parthasarathi and Sharpe, Timothy and Kohl, Bastian and Hiller, Sebastian. (2019) Two-state folding of the outer membrane protein X into a lipid bilayer membrane. Angewandte Chemie International Edition, 58 (9). pp. 2665-2669.

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Official URL: https://edoc.unibas.ch/68406/

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Folding and insertion of β-barrel membrane proteins into native membranes is efficiently catalyzed by β-barrel assembly machineries. Understanding this catalysis requires a detailed description of the corresponding uncatalyzed folding mechanisms, which however have so far remained largely unclear. Here, we resolve folding and membrane insertion of the E. coli outer membrane protein X (OmpX) into 1,2-didecanoyl-sn-glycero-3-phosphocholine (PC10:0) membranes at the atomic level. By combining four different experimental techniques, we correlate global folding kinetics with global and local hydrogen bond formation kinetics. Under a well-defined reaction condition, these processes follow single-exponential velocity laws, with rate constants identical within experimental error. The data thus establish at atomic resolution that OmpX folds and inserts into the lipid bilayer of PC10:0 liposomes by a two-state mechanism.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Hiller)
UniBasel Contributors:Hiller Odermatt, Sebastian and Sharpe, Timothy and Kohl, Bastian and Rath, Parthasarathi
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:08 Feb 2020 15:06
Deposited On:16 Dec 2019 15:36

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