8OO1
Wide inward-open liganded UraA in complex with a conformation-selective synthetic nanobody
Summary for 8OO1
| Entry DOI | 10.2210/pdb8oo1/pdb |
| Related | 8OMZ |
| Descriptor | Uracil permease, Sy45, PENTAETHYLENE GLYCOL, ... (6 entities in total) |
| Functional Keywords | slc23, uracil transporter, uraa, membrane protein, sybody, nanobody |
| Biological source | Escherichia coli O157:H7 More |
| Total number of polymer chains | 4 |
| Total formula weight | 128570.21 |
| Authors | Kuhn, B.T.,Geertsma, E.R. (deposition date: 2023-04-04, release date: 2024-04-10, Last modification date: 2024-10-23) |
| Primary citation | Kuhn, B.T.,Zoller, J.,Zimmermann, I.,Gemeinhardt, T.,Ozkul, D.H.,Langer, J.D.,Seeger, M.A.,Geertsma, E.R. Interdomain-linkers control conformational transitions in the SLC23 elevator transporter UraA. Nat Commun, 15:7518-7518, 2024 Cited by PubMed Abstract: Uptake of nucleobases and ascorbate is an essential process in all living organisms mediated by SLC23 transport proteins. These transmembrane carriers operate via the elevator alternating-access mechanism, and are composed of two rigid domains whose relative motion drives transport. The lack of large conformational changes within these domains suggests that the interdomain-linkers act as flexible tethers. Here, we show that interdomain-linkers are not mere tethers, but have a key regulatory role in dictating the conformational space of the transporter and defining the rotation axis of the mobile transport domain. By resolving a wide inward-open conformation of the SLC23 elevator transporter UraA and combining biochemical studies using a synthetic nanobody as conformational probe with hydrogen-deuterium exchange mass spectrometry, we demonstrate that interdomain-linkers control the function of transport proteins by influencing substrate affinity and transport rate. These findings open the possibility to allosterically modulate the activity of elevator proteins by targeting their linkers. PubMed: 39209842DOI: 10.1038/s41467-024-51814-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.7 Å) |
Structure validation
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