TY  - JOUR
A1  - Gopinath, Aathira
A1  - Joseph, Benesh
T1  - Conformational flexibility of the protein insertase BamA in the native asymmetric bilayer elucidated by ESR spectroscopy
T2  - Angewandte Chemie. International edition
N2  - The β-barrel assembly machinery (BAM) consisting of the central β-barrel BamA and four other lipoproteins mediates the folding of the majority of the outer membrane proteins. BamA is placed in an asymmetric bilayer and its lateral gate is suggested to be the functional hotspot. Here we used in situ pulsed electron-electron double resonance spectroscopy to characterize BamA in the native outer membrane. In the detergent micelles, the data is consistent with mainly an inward-open conformation of BamA. The native membrane considerably enhanced the conformational heterogeneity. The lateral gate and the extracellular loop 3 exist in an equilibrium between different conformations. The outer membrane provides a favorable environment for occupying multiple conformational states independent of the lipoproteins. Our results reveal a highly dynamic behavior of the lateral gate and other key structural elements and provide direct evidence for the conformational modulation of a membrane protein in situ.
KW  - conformational dynamics
KW  - membrane proteins
KW  - PELDOR/DEER spectroscopy
KW  - protein structures
KW  - structural biology
Y1  - 2021
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/75152
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-751523
SN  - 1521-3773
N1  - This work was financially supported through the Emmy Noether program (JO 1428/1-1) and a large equipment funding (438280639) from the Deutsche Forschungsgemeinschaft and the Science Funding from Johanna Quandt Young Academy at Goethe to B.J. Open Access funding enabled and organized by Projekt DEAL.
VL  - 61
IS  - 2, art. e202113448
SP  - 1
EP  - 6
PB  - Wiley-VCH
CY  - Weinheim
ER  -