Fig. 4: Divergent evolution of carotenoid binding in microbial rhodopsin. | Communications Biology

Fig. 4: Divergent evolution of carotenoid binding in microbial rhodopsin.

From: Carotenoid binding in Gloeobacteria rhodopsin provides insights into divergent evolution of xanthorhodopsin types

Fig. 4

a Multiple sequences alignment (MSA) calculated by Bayesian method for evolutionary substitution model of GR (pdb:6nwd) among 150 homologs. DTE motif is almost wholly conserved, while CLM motif showed Gly178 is replaced either bulky residue Trp or aromatic ring residue Phe, and at the same time Ser 181 is either replaced with tiny residue Gly or Ala, CAM motif showed completely conserved of retinal binding pocket Trp 222, and Pro 226, which suggests that this non-polar helix kink residue is essential. b The phylogenetic tree xanthorhodopsin, actinorhodopsin, bacteriorhodopsin, and proteorhodopsin, including dinoflagellate proteorhodopsin. XR showed evolutional closer distance to actinorhodopsin compared to proteorhodopsin. c One-to-one sequence alignment of dinoflagellate Pyrocis lununa rhodopsin and GR, Gly178 was replaced by Trp, and polar residue T179 and Ser181 were replaced by non-polar small alanine. d UV–vis spectra of purified Pyrocis lununa rhodopsin and GR, Pyro-rhodopsin showed maximum absorption at 515 nm in the more blue-green region compared to GR 543 nm. e The proton pumping of expressed GR and Pyro-rhodopsin in E. coli cells with the same protein concentration was calculated.

Back to article page