2onj

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2onj, resolution 3.400Å

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

Overview

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.

About this Structure

2ONJ is a Single protein structure of sequence from Staphylococcus aureus with NA and ANP as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP., Dawson RJ, Locher KP, FEBS Lett. 2007 Mar 6;581(5):935-8. Epub 2007 Feb 7. PMID:17303126

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