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Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP‐PNP
Author(s) -
Dawson Roger J.P.,
Locher Kaspar P.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.01.073
Subject(s) - transporter , atp binding cassette transporter , staphylococcus aureus , multiple drug resistance , adenosine triphosphate , chemistry , transmembrane protein , biochemistry , biology , biophysics , receptor , antibiotics , bacteria , gene , genetics
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′‐(β,γ‐imido)triphosphate (AMP‐PNP) at 3.4 Å 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.