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

被引：329

作者：

Dawson, Roger J. P. ^{[1
]}

Locher, Kaspar P. ^{[1
]}

机构：

[1] ETH, Inst Mol Biol & Biophys, CH-8093 Zurich, Switzerland

来源：

FEBS LETTERS | 2007年 / 581卷 / 05期

关键词：

transport protein; multidrug ABC transporter; AMP-PNP; ATP-bound state; outward-facing conformation; Mdr1;

D O I：

10.1016/j.febslet.2007.01.073

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 3.4 angstrom 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. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：935 / 938

页数：4

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