7EKL

Mitochondrial outer membrane protein

7EKL の概要

• エントリーDOI: 10.2210/pdb7ekl/pdb
• EMDBエントリー: 31169
• 分子名称: ATP-binding cassette sub-family B member 6, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: mitochondrial outer membrane protein, membrane protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 189009.33

構造登録者

Zhang, S.S. (登録日: 2021-04-05, 公開日: 2021-08-25, 最終更新日: 2024-06-05)

主引用文献

Song, G.,Zhang, S.,Tian, M.,Zhang, L.,Guo, R.,Zhuo, W.,Yang, M.
Molecular insights into the human ABCB6 transporter.
Cell Discov, 7:55-55, 2021

PubMed 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 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.

PubMed: 34312373
DOI: 10.1038/s41421-021-00284-z

実験手法

ELECTRON MICROSCOPY (3.5 Å)