Characterization of an archaeal photoreceptor/transducer complex from Natronomonas pharaonis assembled within styrene-maleic acid lipid particles
| Autor(en): | Voskoboynikova, N. Mosslehy, W. Colbasevici, A. Ismagulova, T. T. Bagrov, D. V. Akovantseva, A. A. Timashev, P. S. Mulkidjanian, A. Y. Bagratashvili, V. N. Shaitan, K. V. Kirpichnikov, M. P. Steinhoff, H. -J. |
Stichwörter: | Chemistry; Chemistry, Multidisciplinary; DETERGENT-FREE ISOLATION; DISTANCE MEASUREMENTS; ELECTRON-PARAMAGNETIC-RESONANCE; MEMBRANE-PROTEIN; MICROBIAL RHODOPSINS; MOLECULE HEIGHT MEASUREMENTS; PROTEIN-COUPLED RECEPTORS; SENSORY-RHODOPSIN-II; SIGNAL-TRANSDUCTION; VIBRATIONAL ANALYSIS | Erscheinungsdatum: | 2017 | Herausgeber: | ROYAL SOC CHEMISTRY | Journal: | RSC ADVANCES | Volumen: | 7 | Ausgabe: | 81 | Startseite: | 51324 | Seitenende: | 51334 | Zusammenfassung: | The styrene-maleic acid (SMA) copolymers enable a detergent-free extraction of membrane proteins from lipid bilayers yielding stable water-soluble nanocontainers with lipid-encased proteins. Here, we demonstrate the ability of the SMA copolymer to extract a complex of interacting membrane proteins from proteoliposomes, namely the archaeal sensory rhodopsin II from Natronomonas pharaonis, NpSRII, in complex with its transducer, NpHtrII. The NpSRII/NpHtrII complexes retained their structural integrity within SMA lipid particles as revealed by diverse biophysical techniques. Pulse electron paramagnetic resonance data showed the SMA-encased NpSRII/NpHtrII complexes as native-like 2 : 2 dimers with a distance between NpSRII sites 159 according to the ``V''-shaped conformation found in a crystal structure. |
DOI: | 10.1039/c7ra10756k |
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geprüft am 15.05.2024
