7D7N
Cryo-EM structure of human ABCB6 transporter
7D7N の概要
| エントリーDOI | 10.2210/pdb7d7n/pdb |
| EMDBエントリー | 30609 |
| 分子名称 | ATP-binding cassette sub-family B member 6, mitochondrial (1 entity in total) |
| 機能のキーワード | transporter, dimer, porphyrins, heme, 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 | 187948.34 |
| 構造登録者 | Wang, C.,Cao, C.,Wang, N.,Wang, X.,Zhang, X.C. (登録日: 2020-10-05, 公開日: 2020-10-21, 最終更新日: 2024-03-27) |
| 主引用文献 | Wang, C.,Cao, C.,Wang, N.,Wang, X.,Wang, X.,Zhang, X.C. Cryo-electron microscopy structure of human ABCB6 transporter. Protein Sci., 29:2363-2374, 2020 Cited by PubMed Abstract: Human ATP-binding cassette transporter 6 of subfamily B (ABCB6) is an ABC transporter involved in the translocation toxic metals and anti-cancer drugs. Using cryo-electron microscopy, we determined the molecular structure of full-length ABCB6 in an apo state. The structure of ABCB6 unravels the architecture of a full-length ABCB transporter that harbors two N-terminal transmembrane domains which is indispensable for its ATPase activity in our in vitro assay. A slit-like substrate binding pocket of ABCB6 may accommodate the planar shape of porphyrins, and the existence of a secondary cavity near the mitochondrial intermembrane space side would further facilitate substrate release. Furthermore, the ATPase activity of ABCB6 stimulated with a variety of porphyrin substrates showed different profiles in the presence of glutathione (GSH), suggesting the action of a distinct substrate translocation mechanism depending on the use of GSH as a cofactor. PubMed: 33007128DOI: 10.1002/pro.3960 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (5.2 Å) |
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