The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
Role of the conserved NPxxY(x) 5,6 F motif in the rhodopsin ground state and during activation
Open accessAbstract
In the G protein-coupled receptor rhodopsin, the conserved NPxxY(x) 5,6 F motif connects the transmembrane helix VII and the cytoplasmic helix 8. The less geometrically constrained retinal analogue 9-demethyl-retinal prevents efficient transformation of rhodopsin to signaling metarhodopsin (Meta) II after retinal photoisomerization. Here, we demonstrate that Ala replacement mutations within the NPxxY(x) 5,6 F domain, which eliminate an interaction between aromatic residues Y306 and F313, allow formation of Meta II despite the presence of 9-demethyl-retinal. Also a disulfide bond linking residues 306 and 313 in the 9-demethyl-retinal-reconstituted mutant Y306C/F313C/C316S prevented Meta II formation, whereas the reduced form of the mutant readily transformed to Meta II after illumination. These observations suggest that the interaction between residues 306 and 313 is disrupted during the Meta I/Meta II transition. However, this enhancement in Meta II formation is not reflected in the G protein activation, which is dramatically reduced for these mutants, suggesting that changes in the Y306–F313 interaction also lead to a proper realigning of helix 8 after photoisomerization. The E134Q mutation, located in the second conserved motif, D(E)RY, rescues activity in 9-demethyl-retinal-reconstituted mutants to different degrees, depending on the position of the Ala replacement in the NPxxY(x) 5,6 F motif, thus revealing distinct roles for the NP and Y(x) 5,6 F portions. Our studies underscore the importance of the NPxxY(x) 5,6 F and D(E)RY motifs in providing structural constraints in rhodopsin that rearrange in response to photoisomerization during formation of the G protein-activating Meta II. The dual control of the structural rearrangements secures reliable transformation of quiescent rhodopsin to activating Meta II.
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Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor
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Self-citationRequirement of Rigid-Body Motion of Transmembrane Helices for Light Activation of Rhodopsin
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Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin.
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Functional role of internal water molecules in rhodopsin revealed by x-ray crystallography
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Self-citationActivation of rhodopsin: new insights from structural and biochemical studies
Okada, T., Ernst, O. P., Palczewski, K., & Hofmann, K. P. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01799-6 · Cited by 413
Self-citationRhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F
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Rhodopsin: Structural Basis of Molecular Physiology
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Cited by
Crystal structure of opsin in its G-protein-interacting conformation
Scheerer, P., Park, J. H., Hildebrand, P. W., Kim, Y. J., Krauß, N., Choe, H.-W., Hofmann, K. P., & Ernst, O. P. (2008) · Nature · doi:10.1038/nature07330 · Cited by 1,059
Self-citationNichols, D. E., & Nichols, C. D. (2008) · Chemical Reviews · doi:10.1021/cr078224o · Cited by 895
G Protein–Coupled Receptor Rhodopsin
Palczewski, K. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142743 · Cited by 764
Self-citationA G protein-coupled receptor at work: the rhodopsin model
Hofmann, K. P., Scheerer, P., Hildebrand, P. W., Choe, H.-W., Park, J. H., Heck, M., & Ernst, O. P. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.07.005 · Cited by 376
Self-citationAngel, T. E., Chance, M. R., & Palczewski, K. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903545106 · Cited by 235
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Metadata
- Authors
- Fritze, O., Filipek, S., Kuksa, V., Palczewski, K., Hofmann, K. P., & Ernst, O. P.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2003-02-24
- Volume
- 100
- Issue
- 5
- Pages
- 2290-2295
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1993677150
- Cited by
- 358
- References
- 36
- FWCI
- 5.79
- Type
- journal article
- Language
- en
- Open access
- green
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