Literature DB >> 17303126

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

Roger J P Dawson1, Kaspar P Locher.   

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.

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Year:  2007        PMID： 17303126     DOI： 10.1016/j.febslet.2007.01.073

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  161 in total

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