2015
DOI: 10.1186/s13062-015-0091-4
|View full text |Cite
|
Sign up to set email alerts
|

Eukaryotic G protein-coupled receptors as descendants of prokaryotic sodium-translocating rhodopsins

Abstract: Microbial rhodopsins and G-protein coupled receptors (GPCRs, which include animal rhodopsins) are two distinct (super) families of heptahelical (7TM) membrane proteins that share obvious structural similarities but no significant sequence similarity. Comparison of the recently solved high-resolution structures of the sodium-translocating bacterial rhodopsin and various Na+-binding GPCRs revealed striking similarity of their sodium-binding sites. This similarity allowed us to construct a structure-guided sequen… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

0
41
0
1

Year Published

2016
2016
2021
2021

Publication Types

Select...
5
2
1

Relationship

1
7

Authors

Journals

citations
Cited by 43 publications
(42 citation statements)
references
References 98 publications
(241 reference statements)
0
41
0
1
Order By: Relevance
“…Moreover, in 2015 the evolutional relationship of microbial light-driven Na + pumps and class A G protein-coupled receptors (GPCRs) was studied, based on the existing structures of the ground state of KR2 55 . Presented here structure of the O-state with Na + bound inside the protein supports the high similarity of the Na + binding sites in KR2 and GPCRs.…”
Section: Supplementary Textmentioning
confidence: 99%
“…Moreover, in 2015 the evolutional relationship of microbial light-driven Na + pumps and class A G protein-coupled receptors (GPCRs) was studied, based on the existing structures of the ground state of KR2 55 . Presented here structure of the O-state with Na + bound inside the protein supports the high similarity of the Na + binding sites in KR2 and GPCRs.…”
Section: Supplementary Textmentioning
confidence: 99%
“…Biologists have been seeking evidence to solve the long‐standing question of the common ancestry of these two highly diverged superfamilies of seven transmembrane sensory proteins, rhodopsins, and bacteriorhodopsins. Shalaeva et al () propose a common ancestry for sodium‐translocating bacteriorhodopsins and various sodium ion‐binding GPCRs, given their common ability to bind sodium ions (Shalaeva et al ). Depending on how limited the functionality of rhodopsin‐like GPCRs in dinoflagellates is, the prevalence of proteorhodopsins may point toward their complementary function as energy generators.…”
Section: Discussionmentioning
confidence: 99%
“…4 In addition, NpSRII is distantly related to G-protein coupled receptors (GPCRs) including visual rhodopsins. 5 Similar to other rhodopsins, NpSRII comprises seven transmembrane helices (A-G) with a retinal chromophore covalently bound to a conserved lysine residue of helix G via a protonated Schiff base. In membranes, NpSRII interacts with its cognate transducer (NpHtrII), which consists of a membrane-embedded N-terminal domain with two transmembrane a-helices, TM1 and TM2, and an elongated ahelical coiled-coil cytoplasmic signalling domain that protrudes into the cytoplasm by $26 nm.…”
Section: Introductionmentioning
confidence: 99%