期刊
FEBS LETTERS
卷 581, 期 5, 页码 935-938出版社
WILEY
DOI: 10.1016/j.febslet.2007.01.073
关键词
transport protein; multidrug ABC transporter; AMP-PNP; ATP-bound state; outward-facing conformation; Mdr1
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.
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