This title appears in the Scientific Report :
2022
Please use the identifier:
http://hdl.handle.net/2128/30912 in citations.
Please use the identifier: http://dx.doi.org/10.1039/D2RA00604A in citations.
Mapping the helix arrangement of the reconstituted ETR1 ethylene receptor transmembrane domain by EPR spectroscopy
Mapping the helix arrangement of the reconstituted ETR1 ethylene receptor transmembrane domain by EPR spectroscopy
The plant ethylene receptor ETR1 is a key player in the perception of the phytohormone and subsequent downstream ethylene signal transmission, crucial for processes such as ripening, senescence and abscission. However, to date, there is sparse structural knowledge about the transmembrane sensor doma...
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Personal Name(s): | Kugele, Anandi |
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Uzun, Buket / Müller, Lena / Schott-Verdugo, Stephan / Gohlke, Holger / Groth, Georg (Corresponding author) / Drescher, Malte (Corresponding author) | |
Contributing Institute: |
Bioinformatik; IBG-4 Strukturbiochemie; IBI-7 John von Neumann - Institut für Computing; NIC Jülich Supercomputing Center; JSC |
Published in: | RSC Advances, 12 (2022) S. 7352 - 7356 |
Imprint: |
London
RSC Publishing
2022
|
DOI: |
10.1039/D2RA00604A |
Document Type: |
Journal Article |
Research Program: |
Molecular Information Processing in Cellular Systems Forschergruppe Gohlke Utilization of renewable carbon and energy sources and engineering of ecosystem functions Biological and environmental resources for sustainable use Domain-Specific Simulation & Data Life Cycle Labs (SDLs) and Research Groups |
Link: |
OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://dx.doi.org/10.1039/D2RA00604A in citations.
The plant ethylene receptor ETR1 is a key player in the perception of the phytohormone and subsequent downstream ethylene signal transmission, crucial for processes such as ripening, senescence and abscission. However, to date, there is sparse structural knowledge about the transmembrane sensor domain (TMD) of ETR1 that is responsible for the binding of the plant hormone and initiates the downstream signal transmission. Sequence information and ab initio modelling suggest that the TMD consists of three transmembrane helices. Here, we combined site-directed spin labelling with electron paramagnetic resonance spectroscopy and obtained distance restraints for liposome-reconstituted ETR1_TMD on the orientation and arrangement of the transmembrane helices. We used these data to scrutinize different computational structure predictions of the TMD. |