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-Structure paper
タイトル | Gating by ionic strength and safety check by cyclic-di-AMP in the ABC transporter OpuA. |
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ジャーナル・号・ページ | Sci Adv, Vol. 6, Issue 47, Year 2020 |
掲載日 | 2020年11月18日 |
著者 | Hendrik R Sikkema / Marco van den Noort / Jan Rheinberger / Marijn de Boer / Sabrina T Krepel / Gea K Schuurman-Wolters / Cristina Paulino / Bert Poolman / |
PubMed 要旨 | (Micro)organisms are exposed to fluctuating environmental conditions, and adaptation to stress is essential for survival. Increased osmolality (hypertonicity) causes outflow of water and loss of ...(Micro)organisms are exposed to fluctuating environmental conditions, and adaptation to stress is essential for survival. Increased osmolality (hypertonicity) causes outflow of water and loss of turgor and is dangerous if the cell is not capable of rapidly restoring its volume. The osmoregulatory adenosine triphosphate-binding cassette transporter OpuA restores the cell volume by accumulating large amounts of compatible solute. OpuA is gated by ionic strength and inhibited by the second messenger cyclic-di-AMP, a molecule recently shown to affect many cellular processes. Despite the master regulatory role of cyclic-di-AMP, structural and functional insights into how the second messenger regulates (transport) proteins on the molecular level are lacking. Here, we present high-resolution cryo-electron microscopy structures of OpuA and in vitro activity assays that show how the osmoregulator OpuA is activated by high ionic strength and how cyclic-di-AMP acts as a backstop to prevent unbridled uptake of compatible solutes. |
リンク | Sci Adv / PubMed:33208376 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.3 - 4.5 Å |
構造データ | EMDB-11782, PDB-7ahc: EMDB-11783, PDB-7ahd: EMDB-11784, PDB-7ahe: EMDB-11785: EMDB-11786, PDB-7ahh: |
化合物 | ChemComp-ATP: ChemComp-BET: ChemComp-2BA: ChemComp-ANP: |
由来 |
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キーワード | MEMBRANE PROTEIN / osmoregulation / ABC-transporter / glycine betaine uptake system / cyclic-di-AMP |