6BHU
Cryo-EM structure of ATP-bound, outward-facing bovine multidrug resistance protein 1 (MRP1)
Summary for 6BHU
| Entry DOI | 10.2210/pdb6bhu/pdb |
| Related | 5UJ9 5UJA |
| EMDB information | 7099 |
| Descriptor | Multidrug resistance-associated protein 1, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | abc transporter, multidrug resistance, outward facing, transport protein |
| Biological source | Bos taurus (Bovine) |
| Total number of polymer chains | 1 |
| Total formula weight | 185297.00 |
| Authors | Johnson, Z.L.,Chen, J. (deposition date: 2017-10-31, release date: 2017-12-27, Last modification date: 2024-03-13) |
| Primary citation | Johnson, Z.L.,Chen, J. ATP Binding Enables Substrate Release from Multidrug Resistance Protein 1. Cell, 172:81-89.e10, 2018 Cited by PubMed Abstract: The multidrug resistance protein MRP1 is an ATP-driven pump that confers resistance to chemotherapy. Previously, we have shown that intracellular substrates are recruited to a bipartite binding site when the transporter rests in an inward-facing conformation. A key question remains: how are high-affinity substrates transferred across the membrane and released outside the cell? Using electron cryomicroscopy, we show here that ATP binding opens the transport pathway to the extracellular space and reconfigures the substrate-binding site such that it relinquishes its affinity for substrate. Thus, substrate is released prior to ATP hydrolysis. With this result, we now have a complete description of the conformational cycle that enables substrate transfer in a eukaryotic ABC exporter. PubMed: 29290467DOI: 10.1016/j.cell.2017.12.005 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.14 Å) |
Structure validation
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