This title appears in the Scientific Report :
2023
Please use the identifier:
http://dx.doi.org/10.1039/D3CC02619A in citations.
Please use the identifier: http://dx.doi.org/10.34734/FZJ-2024-00739 in citations.
Functional reconstitution and structural characterization of the plant hormone receptor ETR1 in lipid nanodiscs
Functional reconstitution and structural characterization of the plant hormone receptor ETR1 in lipid nanodiscs
The plant hormone receptor ETR1 regulates many highly relevant agronomic processes. Today, significant functional and structural questions remain unanswered regarding its multi-pass transmembrane sensor domain able to bind and respond to the gaseous plant hormone ethylene at femtomolar concentration...
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Personal Name(s): | Lemke, Moritz |
---|---|
Reiners, Jens / Smits, Sander H. J. / Lakomek, Nils / Groth, Georg (Corresponding author) | |
Contributing Institute: |
Strukturbiochemie; IBI-7 |
Published in: | Chemical communications, 59 (2023) 61, S. 9344 - 9347 |
Imprint: |
Cambridge
Soc.
2023
|
DOI: |
10.1039/D3CC02619A |
DOI: |
10.34734/FZJ-2024-00739 |
Document Type: |
Journal Article |
Research Program: |
SFB 1208: Identität und Dynamik von Membransystemen - von Molekülen bis zu zellulären Funktionen Molecular Information Processing in Cellular Systems |
Link: |
Get full text Published on 2023-07-12. Available in OpenAccess from 2024-07-12. Published on 2023-07-12. Available in OpenAccess from 2024-07-12. |
Publikationsportal JuSER |
Please use the identifier: http://dx.doi.org/10.34734/FZJ-2024-00739 in citations.
The plant hormone receptor ETR1 regulates many highly relevant agronomic processes. Today, significant functional and structural questions remain unanswered regarding its multi-pass transmembrane sensor domain able to bind and respond to the gaseous plant hormone ethylene at femtomolar concentrations. A significant reason for this is the lack of structural data on full-length ETR1 in a lipid environment. Herein, we present the functional reconstitution of recombinant full-length ETR1 purified and solubilized from a bacterial host into lipid nanodiscs, allowing the study of the purified plant receptor for the first time in a detergent-free membrane-like environment. |