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Crystal structure of jumping spider rhodopsin-1 as a light sensitive GPCR
Light-sensitive G protein-coupled receptors (GPCRs)—rhodopsins—absorb photons to isomerize their covalently bound retinal, triggering conformational changes that result in downstream signaling cascades. Monostable rhodopsins release retinal upon isomerization as opposed to the retinal in bistable rh...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
National Academy of Sciences
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6642406/ https://www.ncbi.nlm.nih.gov/pubmed/31249143 http://dx.doi.org/10.1073/pnas.1902192116 |
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author | Varma, Niranjan Mutt, Eshita Mühle, Jonas Panneels, Valérie Terakita, Akihisa Deupi, Xavier Nogly, Przemyslaw Schertler, Gebhard F. X. Lesca, Elena |
author_facet | Varma, Niranjan Mutt, Eshita Mühle, Jonas Panneels, Valérie Terakita, Akihisa Deupi, Xavier Nogly, Przemyslaw Schertler, Gebhard F. X. Lesca, Elena |
author_sort | Varma, Niranjan |
collection | PubMed |
description | Light-sensitive G protein-coupled receptors (GPCRs)—rhodopsins—absorb photons to isomerize their covalently bound retinal, triggering conformational changes that result in downstream signaling cascades. Monostable rhodopsins release retinal upon isomerization as opposed to the retinal in bistable rhodopsins that “reisomerize” upon absorption of a second photon. Understanding the mechanistic differences between these light-sensitive GPCRs has been hindered by the scarcity of recombinant models of the latter. Here, we reveal the high-resolution crystal structure of a recombinant bistable rhodopsin, jumping spider rhodopsin-1, bound to the inverse agonist 9-cis retinal. We observe a water-mediated network around the ligand hinting toward the basis of their bistable nature. In contrast to bovine rhodopsin (monostable), the transmembrane bundle of jumping spider rhodopsin-1 as well that of the bistable squid rhodopsin adopts a more “activation-ready” conformation often observed in other nonphotosensitive class A GPCRs. These similarities suggest the role of jumping spider rhodopsin-1 as a potential model system in the study of the structure–function relationship of both photosensitive and nonphotosensitive class A GPCRs. |
format | Online Article Text |
id | pubmed-6642406 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | National Academy of Sciences |
record_format | MEDLINE/PubMed |
spelling | pubmed-66424062019-07-25 Crystal structure of jumping spider rhodopsin-1 as a light sensitive GPCR Varma, Niranjan Mutt, Eshita Mühle, Jonas Panneels, Valérie Terakita, Akihisa Deupi, Xavier Nogly, Przemyslaw Schertler, Gebhard F. X. Lesca, Elena Proc Natl Acad Sci U S A PNAS Plus Light-sensitive G protein-coupled receptors (GPCRs)—rhodopsins—absorb photons to isomerize their covalently bound retinal, triggering conformational changes that result in downstream signaling cascades. Monostable rhodopsins release retinal upon isomerization as opposed to the retinal in bistable rhodopsins that “reisomerize” upon absorption of a second photon. Understanding the mechanistic differences between these light-sensitive GPCRs has been hindered by the scarcity of recombinant models of the latter. Here, we reveal the high-resolution crystal structure of a recombinant bistable rhodopsin, jumping spider rhodopsin-1, bound to the inverse agonist 9-cis retinal. We observe a water-mediated network around the ligand hinting toward the basis of their bistable nature. In contrast to bovine rhodopsin (monostable), the transmembrane bundle of jumping spider rhodopsin-1 as well that of the bistable squid rhodopsin adopts a more “activation-ready” conformation often observed in other nonphotosensitive class A GPCRs. These similarities suggest the role of jumping spider rhodopsin-1 as a potential model system in the study of the structure–function relationship of both photosensitive and nonphotosensitive class A GPCRs. National Academy of Sciences 2019-07-16 2019-06-28 /pmc/articles/PMC6642406/ /pubmed/31249143 http://dx.doi.org/10.1073/pnas.1902192116 Text en Copyright © 2019 the Author(s). Published by PNAS. https://creativecommons.org/licenses/by-nc-nd/4.0/ https://creativecommons.org/licenses/by-nc-nd/4.0/This open access article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND) (https://creativecommons.org/licenses/by-nc-nd/4.0/) . |
spellingShingle | PNAS Plus Varma, Niranjan Mutt, Eshita Mühle, Jonas Panneels, Valérie Terakita, Akihisa Deupi, Xavier Nogly, Przemyslaw Schertler, Gebhard F. X. Lesca, Elena Crystal structure of jumping spider rhodopsin-1 as a light sensitive GPCR |
title | Crystal structure of jumping spider rhodopsin-1 as a light sensitive GPCR |
title_full | Crystal structure of jumping spider rhodopsin-1 as a light sensitive GPCR |
title_fullStr | Crystal structure of jumping spider rhodopsin-1 as a light sensitive GPCR |
title_full_unstemmed | Crystal structure of jumping spider rhodopsin-1 as a light sensitive GPCR |
title_short | Crystal structure of jumping spider rhodopsin-1 as a light sensitive GPCR |
title_sort | crystal structure of jumping spider rhodopsin-1 as a light sensitive gpcr |
topic | PNAS Plus |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6642406/ https://www.ncbi.nlm.nih.gov/pubmed/31249143 http://dx.doi.org/10.1073/pnas.1902192116 |
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