2ONJ

Structure of the multidrug ABC transporter Sav1866 from S. aureus in complex with AMP-PNP

2ONJ の概要

• エントリーDOI: 10.2210/pdb2onj/pdb
• 分子名称: Multidrug export ATP-binding/permease protein SAV1866, SODIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total)
• 機能のキーワード: integral membrane protein, transport protein, hydrolase
• 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: 130972.28

構造登録者

Dawson, R.J.P.,Locher, K.P. (登録日: 2007-01-24, 公開日: 2007-03-13, 最終更新日: 2023-12-27)

主引用文献

Dawson, R.J.P.,Locher, K.P.
Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP.
Febs Lett., 581:935-938, 2007

PubMed Abstract: Staphylococcus aureus Sav1866 is a bacterial homolog of the human ABC transporter Mdr1 that causes multidrug resistance in cancer cells. We report the crystal structure of Sav1866 in complex with adenosine-5'-(beta,gamma-imido)triphosphate (AMP-PNP) at 3.4A resolution and compare it with the previously determined structure of Sav1866 with bound ADP. Besides differences in the ATP-binding sites, no significant conformational changes were observed. The results confirm that the ATP-bound state of multidrug ABC transporters is coupled to an outward-facing conformation of the transmembrane domains.

PubMed: 17303126
DOI: 10.1016/j.febslet.2007.01.073

実験手法

X-RAY DIFFRACTION (3.4 Å)