Low-resolution structure of the full-length barley (Hordeum vulgare) SGT1 protein in solution, obtained using small-angle X-ray scattering.
SGT1 is an evolutionarily conserved eukaryotic protein involved in many important cellular processes. In plants, SGT1 is involved in resistance to disease. In a low ionic strength environment, the SGT1 protein tends to form dimers. The protein consists of three structurally independent domains (the...
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Public Library of Science (PLoS)
2014-01-01
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| Series: | PLoS ONE |
| Online Access: | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0093313&type=printable |
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| author | Michał Taube Joanna R Pieńkowska Artur Jarmołowski Maciej Kozak |
| author_facet | Michał Taube Joanna R Pieńkowska Artur Jarmołowski Maciej Kozak |
| author_sort | Michał Taube |
| collection | DOAJ |
| description | SGT1 is an evolutionarily conserved eukaryotic protein involved in many important cellular processes. In plants, SGT1 is involved in resistance to disease. In a low ionic strength environment, the SGT1 protein tends to form dimers. The protein consists of three structurally independent domains (the tetratricopeptide repeats domain (TPR), the CHORD- and SGT1-containing domain (CS), and the SGT1-specific domain (SGS)), and two less conserved variable regions (VR1 and VR2). In the present study, we provide the low-resolution structure of the barley (Hordeum vulgare) SGT1 protein in solution and its dimer/monomer equilibrium using small-angle scattering of synchrotron radiation, ab-initio modeling and circular dichroism spectroscopy. The multivariate curve resolution least-square method (MCR-ALS) was applied to separate the scattering data of the monomeric and dimeric species from a complex mixture. The models of the barley SGT1 dimer and monomer were formulated using rigid body modeling with ab-initio structure prediction. Both oligomeric forms of barley SGT1 have elongated shapes with unfolded inter-domain regions. Circular dichroism spectroscopy confirmed that the barley SGT1 protein had a modular architecture, with an α-helical TPR domain, a β-sheet sandwich CS domain, and a disordered SGS domain separated by VR1 and VR2 regions. Using molecular docking and ab-initio protein structure prediction, a model of dimerization of the TPR domains was proposed. |
| format | Article |
| id | doaj-art-79dfa9a9d3aa479796bd5f349e0d5a0a |
| institution | OA Journals |
| issn | 1932-6203 |
| language | English |
| publishDate | 2014-01-01 |
| publisher | Public Library of Science (PLoS) |
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| series | PLoS ONE |
| spelling | doaj-art-79dfa9a9d3aa479796bd5f349e0d5a0a2025-08-20T02:14:42ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0194e9331310.1371/journal.pone.0093313Low-resolution structure of the full-length barley (Hordeum vulgare) SGT1 protein in solution, obtained using small-angle X-ray scattering.Michał TaubeJoanna R PieńkowskaArtur JarmołowskiMaciej KozakSGT1 is an evolutionarily conserved eukaryotic protein involved in many important cellular processes. In plants, SGT1 is involved in resistance to disease. In a low ionic strength environment, the SGT1 protein tends to form dimers. The protein consists of three structurally independent domains (the tetratricopeptide repeats domain (TPR), the CHORD- and SGT1-containing domain (CS), and the SGT1-specific domain (SGS)), and two less conserved variable regions (VR1 and VR2). In the present study, we provide the low-resolution structure of the barley (Hordeum vulgare) SGT1 protein in solution and its dimer/monomer equilibrium using small-angle scattering of synchrotron radiation, ab-initio modeling and circular dichroism spectroscopy. The multivariate curve resolution least-square method (MCR-ALS) was applied to separate the scattering data of the monomeric and dimeric species from a complex mixture. The models of the barley SGT1 dimer and monomer were formulated using rigid body modeling with ab-initio structure prediction. Both oligomeric forms of barley SGT1 have elongated shapes with unfolded inter-domain regions. Circular dichroism spectroscopy confirmed that the barley SGT1 protein had a modular architecture, with an α-helical TPR domain, a β-sheet sandwich CS domain, and a disordered SGS domain separated by VR1 and VR2 regions. Using molecular docking and ab-initio protein structure prediction, a model of dimerization of the TPR domains was proposed.https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0093313&type=printable |
| spellingShingle | Michał Taube Joanna R Pieńkowska Artur Jarmołowski Maciej Kozak Low-resolution structure of the full-length barley (Hordeum vulgare) SGT1 protein in solution, obtained using small-angle X-ray scattering. PLoS ONE |
| title | Low-resolution structure of the full-length barley (Hordeum vulgare) SGT1 protein in solution, obtained using small-angle X-ray scattering. |
| title_full | Low-resolution structure of the full-length barley (Hordeum vulgare) SGT1 protein in solution, obtained using small-angle X-ray scattering. |
| title_fullStr | Low-resolution structure of the full-length barley (Hordeum vulgare) SGT1 protein in solution, obtained using small-angle X-ray scattering. |
| title_full_unstemmed | Low-resolution structure of the full-length barley (Hordeum vulgare) SGT1 protein in solution, obtained using small-angle X-ray scattering. |
| title_short | Low-resolution structure of the full-length barley (Hordeum vulgare) SGT1 protein in solution, obtained using small-angle X-ray scattering. |
| title_sort | low resolution structure of the full length barley hordeum vulgare sgt1 protein in solution obtained using small angle x ray scattering |
| url | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0093313&type=printable |
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