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2HYD

Multidrug ABC transporter SAV1866

2HYD の概要
エントリーDOI10.2210/pdb2hyd/pdb
分子名称ABC transporter homolog, SODIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
機能のキーワードtransport protein
由来する生物種Staphylococcus aureus
細胞内の位置Cell membrane; Multi-pass membrane protein: Q99T13
タンパク質・核酸の鎖数2
化学式量合計130768.31
構造登録者
Dawson, R.J.P.,Locher, K.P. (登録日: 2006-08-05, 公開日: 2006-09-05, 最終更新日: 2024-02-21)
主引用文献Dawson, R.J.,Locher, K.P.
Structure of a bacterial multidrug ABC transporter.
Nature, 443:180-185, 2006
Cited by
PubMed Abstract: Multidrug transporters of the ABC family facilitate the export of diverse cytotoxic drugs across cell membranes. This is clinically relevant, as tumour cells may become resistant to agents used in chemotherapy. To understand the molecular basis of this process, we have determined the 3.0 A crystal structure of a bacterial ABC transporter (Sav1866) from Staphylococcus aureus. The homodimeric protein consists of 12 transmembrane helices in an arrangement that is consistent with cross-linking studies and electron microscopic imaging of the human multidrug resistance protein MDR1, but critically different from that reported for the bacterial lipid flippase MsbA. The observed, outward-facing conformation reflects the ATP-bound state, with the two nucleotide-binding domains in close contact and the two transmembrane domains forming a central cavity--presumably the drug translocation pathway--that is shielded from the inner leaflet of the lipid bilayer and from the cytoplasm, but exposed to the outer leaflet and the extracellular space.
PubMed: 16943773
DOI: 10.1038/nature05155
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3 Å)
構造検証レポート
Validation report summary of 2hyd
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-03-25に公開中

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