Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 116, Issue 29, Pages 14547-14556Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1902192116
Keywords
rhodopsin; bistability; G protein-coupled receptors; retinal; X-ray crystallography
Categories
Funding
- National Centres of Competence in Research Molecular Systems Engineering
- Swiss National Science Foundation [173335, PZ00P3_174169]
- X-Probe ITN [637295]
- Peter und Traudl Engelhorn Stiftung
- European Community's Seventh Framework Program (FP7/2007-2013) [290605]
- Swiss Nanoscience Institute-Nanoargovia Grant [A13.12]
- Japanese Ministry of Education, Culture, Sports, Science and Technology [15H05777]
- Technology Agency (JST) Core Research for Evolutional Science and Technology Grant [JPMJCR1753]
- Grants-in-Aid for Scientific Research [15H05777] Funding Source: KAKEN
- Swiss National Science Foundation (SNF) [PZ00P3_174169] Funding Source: Swiss National Science Foundation (SNF)
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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.
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