Related ArticlesConformation and orientation of the retinyl chromophore in rhodopsin: a critical evaluation of recent NMR data on the basis of theoretical calculations results in a minimum energy structure consistent with all experimental data.
In the absence of a high-resolution diffraction structure, the orientation and conformation of the protonated Schiffs base retinylidinium chromophore of rhodopsin within the opsin matrix has been the subject of much speculation. There have been two recent reliable and precise NMR results that bear on this issue. One involves a determination of the C20-C10 and C20-C11 distances by Verdegem et al. [Biochemistry 38, 11316-11324 (1999)]. The other is the determination of the orientation of the methine C to methyl group vectors C5-C18, C9-C19, and C13-C20 relative to the membrane normal by Gröbner et al. [Nature 405 (6788), 810-813 (2000)]. Using molecular orbital methods that include extensive configuration interaction, we have determined what we propose to be the minimum energy conformation of this chromophore. The above NMR results permit us to check this structure in the C10-C11=C12-C13 region and then to check the global structure via the relative orientation of the three C18, C19, and C20 methyl groups. This method provides a detailed structure and also the orientation for the retinyl chromophore relative to the membrane normal and argues strongly that the protein does not appreciably alter the chromophore geometry from its minimum energy configuration that is nearly planar s-trans at the 6-7 bond. Finally, the chromophore structure and orientation presented in the recently published X-ray diffraction structure is compared with our proposed structure and with the deuterium NMR results.
Rapid three-dimensional MAS NMR spectroscopy at critical sensitivity.
Rapid three-dimensional MAS NMR spectroscopy at critical sensitivity.
Rapid three-dimensional MAS NMR spectroscopy at critical sensitivity.
Angew Chem Int Ed Engl. 2010 Nov 22;49(48):9215-8
Authors: Matsuki Y, Eddy MT, Griffin RG, Herzfeld J
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[NMR paper] Heteronuclear solution-state NMR studies of the chromophore in cyanobacterial phytoch
Heteronuclear solution-state NMR studies of the chromophore in cyanobacterial phytochrome Cph1.
Related Articles Heteronuclear solution-state NMR studies of the chromophore in cyanobacterial phytochrome Cph1.
Biochemistry. 2005 Jun 14;44(23):8244-50
Authors: Strauss HM, Hughes J, Schmieder P
Precise structural information regarding the chromophore binding pocket is essential for an understanding of photochromicity and photoconversion in phytochrome photoreceptors. To this end, we are studying the 59 kDa N-terminal module of the cyanobacterial...
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[NMR paper] Photoreceptor rhodopsin: structural and conformational study of its chromophore 11-ci
Photoreceptor rhodopsin: structural and conformational study of its chromophore 11-cis retinal in oriented membranes by deuterium solid state NMR.
Related Articles Photoreceptor rhodopsin: structural and conformational study of its chromophore 11-cis retinal in oriented membranes by deuterium solid state NMR.
FEBS Lett. 1998 Jan 30;422(2):201-4
Authors: Gröbner G, Choi G, Burnett IJ, Glaubitz C, Verdegem PJ, Lugtenburg J, Watts A
Rhodopsin is the retinal photoreceptor responsible for visual signal transduction. To determine the orientation and...
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[NMR paper] A 1H NMR comparative study of the structure of the critical packing interfaces betwee
A 1H NMR comparative study of the structure of the critical packing interfaces between helix and non-helical region in various ligation states of sperm whale myoglobin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles A 1H NMR comparative study of the structure of the critical packing interfaces between helix and non-helical region in various ligation states of sperm whale myoglobin.
Biochim Biophys Acta. 1997 Nov 14;1343(1):59-66
Authors: Yamamoto Y
NMR signals arising...
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[NMR paper] Protein-chromophore interactions in alpha-crustacyanin, the major blue carotenoprotei
Protein-chromophore interactions in alpha-crustacyanin, the major blue carotenoprotein from the carapace of the lobster, Homarus gammarus. A study by 13C magic angle spinning NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Protein-chromophore interactions in alpha-crustacyanin, the major blue carotenoprotein from the carapace of the lobster, Homarus gammarus. A study by 13C magic angle spinning NMR.
FEBS Lett. 1995 Mar 27;362(1):34-8
Authors: Weesie RJ, Askin D, Jansen FJ, de...
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[NMR paper] NMR constraints on the location of the retinal chromophore in rhodopsin and bathorhod
NMR constraints on the location of the retinal chromophore in rhodopsin and bathorhodopsin.
Related Articles NMR constraints on the location of the retinal chromophore in rhodopsin and bathorhodopsin.
Biochemistry. 1995 Jan 31;34(4):1425-32
Authors: Han M, Smith SO
Rhodopsin is the photoreceptor in vertebrate rod cells responsible for vision at low light intensities. The photoreactive chromophore in rhodopsin is 11-cis-retinal bound to the protein via a protonated Schiff base with Glu113 as the counterion. We have used the observed 13C NMR...
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[NMR paper] Conformation of MeAla6-cyclosporin A by NMR. Relationship of sidechain orientation of
Conformation of MeAla6-cyclosporin A by NMR. Relationship of sidechain orientation of the MeBmt-1, MeLeu-9, and MeLeu-10 residues to immunosuppressive activity.
Related Articles Conformation of MeAla6-cyclosporin A by NMR. Relationship of sidechain orientation of the MeBmt-1, MeLeu-9, and MeLeu-10 residues to immunosuppressive activity.
Int J Pept Protein Res. 1991 May;37(5):351-63
Authors: Gooley PR, Durette PL, Boger J, Armitage IM
MeAla6-cyclosporin A (MeAla6-CsA) is a unique CsA analog that shows weak immunosuppressive activity and yet...