CryoEM structure and small-angle X-ray scattering analyses of porcine retinol-binding protein 3
The vertebrate visual cycle hinges on enzymatically converting all-trans-retinol (at-ROL) into 11-cis-retinal (11c-RAL), the chromophore that binds to opsins in photoreceptors, forming light-responsive pigments. When struck by a photon, these pigments activate the phototransduction pathway and initi...
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The Royal Society
2025-01-01
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| Online Access: | https://royalsocietypublishing.org/doi/10.1098/rsob.240180 |
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| author | Vineeta Kaushik Luca Gessa Nelam Kumar Matyáš Pinkas Mariusz Czarnocki-Cieciura Krzysztof Palczewski Jiří Nováček Humberto Fernandes |
| author_facet | Vineeta Kaushik Luca Gessa Nelam Kumar Matyáš Pinkas Mariusz Czarnocki-Cieciura Krzysztof Palczewski Jiří Nováček Humberto Fernandes |
| author_sort | Vineeta Kaushik |
| collection | DOAJ |
| description | The vertebrate visual cycle hinges on enzymatically converting all-trans-retinol (at-ROL) into 11-cis-retinal (11c-RAL), the chromophore that binds to opsins in photoreceptors, forming light-responsive pigments. When struck by a photon, these pigments activate the phototransduction pathway and initiate the process of vision. The enzymatic isomerization of at-ROL, crucial for restoring the visual pigments and preparing them to receive new light stimuli, relies on various enzymes found in both the photoreceptors and retinal pigment epithelium cells. To function effectively, retinoids must shuttle between these two cell types. Retinol-binding protein 3 (RBP3), located in the interphotoreceptor matrix, probably plays a pivotal role in this transport mechanism. Comprised of four retinoid-binding modules, RBP3 also binds fatty acids, potentially aiding retinal function by facilitating the loading and unloading of different retinoids at specific cell types thereby directing the cycle. In this study, we present a 3.67 Å cryoEM structure of porcine RBP3, along with molecular docking analysis and corroborative in-solution small-angle X-ray scattering data for titration of RBP3 with relevant ligands, that also give insights on RBP3 conformational adaptability. |
| format | Article |
| id | doaj-art-294bcd2d1ffb4382aa030ee3a38e3e8a |
| institution | Kabale University |
| issn | 2046-2441 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | The Royal Society |
| record_format | Article |
| series | Open Biology |
| spelling | doaj-art-294bcd2d1ffb4382aa030ee3a38e3e8a2025-01-22T00:07:47ZengThe Royal SocietyOpen Biology2046-24412025-01-0115110.1098/rsob.240180CryoEM structure and small-angle X-ray scattering analyses of porcine retinol-binding protein 3Vineeta Kaushik0Luca Gessa1Nelam Kumar2Matyáš Pinkas3Mariusz Czarnocki-Cieciura4Krzysztof Palczewski5Jiří Nováček6Humberto Fernandes7Institute of Physical Chemistry, Polish Academy of Sciences , Warsaw, PolandIntegrated Structural Biology Group, International Centre for Translational Eye Research, Institute of Physical Chemistry, Polish Academy of Sciences , Warsaw, PolandIntegrated Structural Biology Group, International Centre for Translational Eye Research, Institute of Physical Chemistry, Polish Academy of Sciences , Warsaw, PolandCEITEC Masaryk University, Kamenice 5 , Brno 62500, Czech RepublicLaboratory of Protein Structure, International Institute of Molecular and Cell Biology , Warsaw, PolandDepartments of Ophthalmology, Chemistry, Physiology & Biophysics, and Molecular Biology & Biochemistry, Gavin Herbert Eye Institute-Center for Translational Vision Research, University of California , Irvine, CA 92697, USACEITEC Masaryk University, Kamenice 5 , Brno 62500, Czech RepublicInstitute of Physical Chemistry, Polish Academy of Sciences , Warsaw, PolandThe vertebrate visual cycle hinges on enzymatically converting all-trans-retinol (at-ROL) into 11-cis-retinal (11c-RAL), the chromophore that binds to opsins in photoreceptors, forming light-responsive pigments. When struck by a photon, these pigments activate the phototransduction pathway and initiate the process of vision. The enzymatic isomerization of at-ROL, crucial for restoring the visual pigments and preparing them to receive new light stimuli, relies on various enzymes found in both the photoreceptors and retinal pigment epithelium cells. To function effectively, retinoids must shuttle between these two cell types. Retinol-binding protein 3 (RBP3), located in the interphotoreceptor matrix, probably plays a pivotal role in this transport mechanism. Comprised of four retinoid-binding modules, RBP3 also binds fatty acids, potentially aiding retinal function by facilitating the loading and unloading of different retinoids at specific cell types thereby directing the cycle. In this study, we present a 3.67 Å cryoEM structure of porcine RBP3, along with molecular docking analysis and corroborative in-solution small-angle X-ray scattering data for titration of RBP3 with relevant ligands, that also give insights on RBP3 conformational adaptability.https://royalsocietypublishing.org/doi/10.1098/rsob.240180RBP3cryoEM structureSAXSconformational changesmolecular docking |
| spellingShingle | Vineeta Kaushik Luca Gessa Nelam Kumar Matyáš Pinkas Mariusz Czarnocki-Cieciura Krzysztof Palczewski Jiří Nováček Humberto Fernandes CryoEM structure and small-angle X-ray scattering analyses of porcine retinol-binding protein 3 Open Biology RBP3 cryoEM structure SAXS conformational changes molecular docking |
| title | CryoEM structure and small-angle X-ray scattering analyses of porcine retinol-binding protein 3 |
| title_full | CryoEM structure and small-angle X-ray scattering analyses of porcine retinol-binding protein 3 |
| title_fullStr | CryoEM structure and small-angle X-ray scattering analyses of porcine retinol-binding protein 3 |
| title_full_unstemmed | CryoEM structure and small-angle X-ray scattering analyses of porcine retinol-binding protein 3 |
| title_short | CryoEM structure and small-angle X-ray scattering analyses of porcine retinol-binding protein 3 |
| title_sort | cryoem structure and small angle x ray scattering analyses of porcine retinol binding protein 3 |
| topic | RBP3 cryoEM structure SAXS conformational changes molecular docking |
| url | https://royalsocietypublishing.org/doi/10.1098/rsob.240180 |
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