7AHD
OpuA (E190Q) occluded
Summary for 7AHD
| Entry DOI | 10.2210/pdb7ahd/pdb |
| EMDB information | 11782 11783 11784 11785 11786 |
| Descriptor | ABC-type proline/glycine betaine transport system ATPase component, ABC transporter permease subunit, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | osmoregulation, abc-transporter, glycine betaine uptake system, membrane protein |
| Biological source | Lactococcus lactis subsp. lactis More |
| Total number of polymer chains | 4 |
| Total formula weight | 219573.54 |
| Authors | Sikkema, H.R.,Rheinberger, J.,Paulino, C.,Poolman, B. (deposition date: 2020-09-24, release date: 2020-11-25, Last modification date: 2023-11-15) |
| Primary citation | Sikkema, H.R.,van den Noort, M.,Rheinberger, J.,de Boer, M.,Krepel, S.T.,Schuurman-Wolters, G.K.,Paulino, C.,Poolman, B. Gating by ionic strength and safety check by cyclic-di-AMP in the ABC transporter OpuA. Sci Adv, 6:-, 2020 Cited by PubMed Abstract: (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. PubMed: 33208376DOI: 10.1126/sciadv.abd7697 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
Download full validation report
