Chemical ScienceBioengineeringPeer-reviewed journal article
Engineering of soluble bacteriorhodopsin
Andrey NikolaeviD, Yaroslav Orlov, Fedor M. TsybroviD, Elizaveta KuznetsovaiD, Pavel ShishkiniD, Alexander KuzminiD, Anatolii MikhailoviD, Yulia S. Nikolaeva, Arina A. AnuchinaiD, Igor V. ChizhoviD, Oleg SemenoviD, Ivan KapranoviD, Valentin I. BorshchevskiyiD, Alina RemeevaiD, Ivan GushchiniD
Abstract
Bacteriorhodopsin is a seven-helical light-driven proton pump and a model membrane protein. Here, we report engineering of soluble analogues of bacteriorhodopsin, NeuroBRs, which bind retinal and photocycle under illumination. We also report the crystallographic structure of NeuroBR_A, determined at anisotropic resolution reaching 1.76 [A], that reveals a conserved chromophore binding pocket and tertiary structure. Our results highlight the power of modern protein engineering approaches and pave the way towards wider development of molecular tools derived from membrane proteins.
- Citations
- 8
- FWCI
- 2.51
- Field percentile
- top 10%
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Proton uptake mechanism in bacteriorhodopsin captured by serial synchrotron crystallography
T. Weinert, P. Skopintsev, … J. Standfuss·bioRxiv·Mar 14, 2019
- Hydroxide Ion Carrier for Proton Pump in Bacteriorhodopsin: Primary Proton Transfer
- Directional proton conductance in bacteriorhodopsin is driven by concentration gradient, not affinity gradient
Z. Ren·bioRxiv·Oct 4, 2021
- Photoinduced isomerization sampling of retinal in bacteriorhodopsin
Z. Ren·bioRxiv·Sep 16, 2021
- Molecular mechanism of light-driven sodium pumping
K. Kovalev, R. Astashkin, … V. Gordeliy·bioRxiv·Jan 29, 2020
- Unraveling the mechanism of proton translocation in the extracellular half-channel of bacteriorhodopsin
Xiaoxia Ge, Marilyn R. Gunner·bioRxiv·Feb 15, 2016