2023
DOI: 10.1039/d2ra07073a
|View full text |Cite|
|
Sign up to set email alerts
|

Convergent evolution of animal and microbial rhodopsins

Abstract: Animal and microbial rhodopsins have common molecular properties (e.g. protein structure, retinal structure, color sensitivity, and photoreaction) while their functions are distinctively different (e.g. GPCRs versus and ion transporters).

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

0
4
0

Year Published

2023
2023
2024
2024

Publication Types

Select...
10

Relationship

1
9

Authors

Journals

citations
Cited by 19 publications
(16 citation statements)
references
References 142 publications
(262 reference statements)
0
4
0
Order By: Relevance
“…While microbial and animal rhodopsins have a similar 7-transmembrane α-helical structure and use a retinal molecule as a chromophore [30], microbial rhodopsins have a broader range of apoprotein molecular structures compared to animal rhodopsins. Microbial rhodopsins comprise all-trans retinal via the protonated Schiff base linkage with a Lys residue positioned at helix G in the dark to absorb visible light [57].…”
Section: Rhodopsinsmentioning
confidence: 99%
“…While microbial and animal rhodopsins have a similar 7-transmembrane α-helical structure and use a retinal molecule as a chromophore [30], microbial rhodopsins have a broader range of apoprotein molecular structures compared to animal rhodopsins. Microbial rhodopsins comprise all-trans retinal via the protonated Schiff base linkage with a Lys residue positioned at helix G in the dark to absorb visible light [57].…”
Section: Rhodopsinsmentioning
confidence: 99%
“…Opsin is a group of seven transmembrane G protein coupled receptors, mainly containing microbial and animal opsins, that covalently binds with a vitamin A based retinaldehyde chromophore. It can be activated by the light ranged from blue to red. , Dronpa can reverse between polymer state and monomer state under cyan light and violet light activation, respectively. , The light-sensitivity of cobalamin-binding domains (CBDs) can mediate the assembly of CarH tetramers in darkness, and dissociate into monomers under green-light. Phytochromes are red or NIR light-sensitive signaling proteins with a broad superfamily such as Cph1, phyA, phyB, and BphP1. These NIR-based optogenetic tools with excellent kinetic properties, hold great promise for remote control of mammalian signaling because of the better light penetration depth …”
Section: Development Of Optogeneticsmentioning
confidence: 99%
“…An increase in the counterion pKa and, subsequently, enhancement of the fluorescence was also observed for the O intermediate of the bacteriorhodopsin photocycle. The O intermediate arises at the last stage of the photocycle (Figure 3 and converts to the ground state of the protein on the timescale of ≈10 ms [65,66]. The main difference between the O intermediate and the ground state is the protonation state of two titratable groups-the D85 counterion and the proton release group [66] located close to the extracellular side of the protein that includes E194, E204, R82, Y83, and surrounding water molecules, as shown in Figure 4c.…”
Section: Fluorescence Properties Of Microbial Rhodopsinsmentioning
confidence: 99%