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Mirror proteorhodopsins
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DOI：10.1038/s42004-023-00884-8.png)
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Abstract
En 中文
Proteorhodopsins (PRs), bacterial light-driven outward proton pumps comprise the first discovered and largest family of rhodopsins, they play a significant role in life on the Earth. A big remaining mystery was that up-to-date there was no described bacterial rhodopsins pumping protons at acidic pH despite the fact that bacteria live in different pH environment. Here we describe conceptually new bacterial rhodopsins which are operating as outward proton pumps at acidic pH. A comprehensive function-structure study of a representative of a new clade of proton pumping rhodopsins which we name mirror proteorhodopsins, from Sphingomonas paucimobilis (SpaR) shows cavity/gate architecture of the proton translocation pathway rather resembling channelrhodopsins than the known rhodopsin proton pumps. Another unique property of mirror proteorhodopsins is that proton pumping is inhibited by a millimolar concentration of zinc. We also show that mirror proteorhodopsins are extensively represented in opportunistic multidrug resistant human pathogens, plant growth-promoting and zinc solubilizing bacteria. They may be of optogenetic interest. Proteorhodopsins act as light-driven outward proton pumps mainly at neutral and alkaline pH, however, mirror proteorhodopsins are known to operate only at acidic pH. Here, the authors report the detailed structural and functional characterization of pH mirror proteorhodopsin SpaR as well as its diverse biological roles.
Keywords:
PSEUDOMONAS-PUTIDA STRAIN
DRIVEN PROTON PUMP
NOSOCOMIAL INFECTIONS
STRUCTURAL INSIGHTS
PANTOEA-AGGLOMERANS
ZINC RESISTANCE
BACTERIORHODOPSIN
RHODOPSIN
RESOLUTION
PROTEIN
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