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TitleATP Binding Enables Substrate Release from Multidrug Resistance Protein 1.
Journal, issue, pagesCell, Vol. 172, Issue 1-2, Page 81-89.e10, Year 2018
Publish dateJan 11, 2018
AuthorsZachary Lee Johnson / Jue Chen /
PubMed AbstractThe 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 ...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.
External linksCell / PubMed:29290467
MethodsEM (single particle)
Resolution3.14 Å
Structure data

7099

6bhu

EMDB-7099, PDB-6bhu:
Cryo-EM structure of ATP-bound, outward-facing bovine multidrug resistance protein 1 (MRP1)
Method: EM (single particle) / Resolution: 3.14 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-MG:
Unknown entry

ChemComp-CLR:
CHOLESTEROL / Cholesterol

Source
  • bos taurus (cattle)
KeywordsTRANSPORT PROTEIN / ABC transporter / multidrug resistance / outward facing

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