Journal: Cell Discov / Year: 2021 Title: Molecular insights into the human ABCB6 transporter. Authors: Guangyuan Song / Sensen Zhang / Mengqi Tian / Laixing Zhang / Runyu Guo / Wei Zhuo / Maojun Yang / Abstract: ABCB6 plays a crucial role in energy-dependent porphyrin transport, drug resistance, toxic metal resistance, porphyrin biosynthesis, protection against stress, and encoding a blood group system ...ABCB6 plays a crucial role in energy-dependent porphyrin transport, drug resistance, toxic metal resistance, porphyrin biosynthesis, protection against stress, and encoding a blood group system Langereis antigen. However, the mechanism underlying porphyrin transport is still unclear. Here, we determined the cryo-electron microscopy (cryo-EM) structures of nanodisc-reconstituted human ABCB6 trapped in an apo-state and an ATP-bound state at resolutions of 3.6 and 3.5 Å, respectively. Our structures reveal a unique loop in the transmembrane domain (TMD) of ABCB6, which divides the TMD into two cavities. It restrains the access of substrates in the inward-facing state and is removed by ATP-driven conformational change. No ligand cavities were observed in the nucleotide-bound state, indicating a state following substrate release but prior to ATP hydrolysis. Structural analyses and functional characterizations suggest an "ATP-switch" model and further reveal the conformational changes of the substrate-binding pockets triggered by the ATP-driven regulation.
History
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Apr 5, 2021
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Header (metadata) release
Aug 25, 2021
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Aug 25, 2021
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Update
Jun 5, 2024
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Current status
Jun 5, 2024
Processing site: PDBj / Status: Released
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