Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET
MxA (myxovirus resistance protein A) is a viral restriction factor whose activity depends on self-assembly into polymeric rings and helical filaments. Here the authors reveal the conformational movements involved in generating torque within polymeric MxA molecules and the dynamic conformational chan...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2017-05-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/ncomms15744 |
| _version_ | 1830299767801905152 |
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| author | Yang Chen Lei Zhang Laura Graf Bing Yu Yue Liu Georg Kochs Yongfang Zhao Song Gao |
| author_facet | Yang Chen Lei Zhang Laura Graf Bing Yu Yue Liu Georg Kochs Yongfang Zhao Song Gao |
| author_sort | Yang Chen |
| collection | DOAJ |
| description | MxA (myxovirus resistance protein A) is a viral restriction factor whose activity depends on self-assembly into polymeric rings and helical filaments. Here the authors reveal the conformational movements involved in generating torque within polymeric MxA molecules and the dynamic conformational changes that occur upon GTP loading and hydrolysis. |
| first_indexed | 2024-12-19T08:15:00Z |
| format | Article |
| id | doaj.art-238a897e890a4cd0ae63f68efa6cfb0a |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-19T08:15:00Z |
| publishDate | 2017-05-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-238a897e890a4cd0ae63f68efa6cfb0a2022-12-21T20:29:31ZengNature PortfolioNature Communications2041-17232017-05-018111110.1038/ncomms15744Conformational dynamics of dynamin-like MxA revealed by single-molecule FRETYang Chen0Lei Zhang1Laura Graf2Bing Yu3Yue Liu4Georg Kochs5Yongfang Zhao6Song Gao7State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer CenterNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesInstitute of Virology, Medical Center, Faculty of Medicine, University of FreiburgState Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer CenterNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesInstitute of Virology, Medical Center, Faculty of Medicine, University of FreiburgNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesState Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer CenterMxA (myxovirus resistance protein A) is a viral restriction factor whose activity depends on self-assembly into polymeric rings and helical filaments. Here the authors reveal the conformational movements involved in generating torque within polymeric MxA molecules and the dynamic conformational changes that occur upon GTP loading and hydrolysis.https://doi.org/10.1038/ncomms15744 |
| spellingShingle | Yang Chen Lei Zhang Laura Graf Bing Yu Yue Liu Georg Kochs Yongfang Zhao Song Gao Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET Nature Communications |
| title | Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET |
| title_full | Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET |
| title_fullStr | Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET |
| title_full_unstemmed | Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET |
| title_short | Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET |
| title_sort | conformational dynamics of dynamin like mxa revealed by single molecule fret |
| url | https://doi.org/10.1038/ncomms15744 |
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