Ionic strength‐dependent conformations of a ubiquitin‐like small archaeal modifier protein (SAMP1) from Haloferax volcanii |
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| Authors: | Kaiqin Ye Shanhui Liao Wen Zhang Kai Fan Xuecheng Zhang Jiahai Zhang Chao Xu Xiaoming Tu |
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| Affiliation: | 1. Hefei National Laboratory for Physical Sciences at Microscale, School of Life Science, University of Science and Technology of China, , Hefei, Anhui, 230026 People's Republic of China;2. Reproductive Medical Center, Nanjing General Hospital of Nanjing Military Command, , Nanjing, 21002 People's Republic of China;3. School of Life Sciences, Anhui University, , Hefei, Anhui, 230039 People's Republic of China;4. Structural Genomics Consortium, University of Toronto, , Toronto, Ontario, M5G 1L7 Canada |
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| Abstract: | Eukaryotic ubiquitin and ubiquitin‐like systems play crucial roles in various cellular biological processes. In this work, we determined the solution structure of SAMP1 from Haloferax volcanii by NMR spectroscopy. Under low ionic conditions, SAMP1 presented two distinct conformations, one folded β‐grasp and the other disordered. Interestingly, SAMP1 underwent a conformational conversion from disorder to order with ion concentration increasing, indicating that the ordered conformation is the functional form of SAMP1 under the physiological condition of H. volcanii. Furthermore, SAMP1 could interact with proteasome‐activating nucleotidase B, supposing a potential role of SAMP1 in the protein degradation pathway mediated by proteasome. |
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| Keywords: | NMR Haloferax volcanii ubiquitin‐like protein SAMP1 protein folding |
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