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Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP‐PNP
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′‐(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.
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Smith, P. C., Karpowich, N., Millen, L., Moody, J. E., Rosen, J., Thomas, P. J., & Hunt, J. F. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00576-2 · Cited by 773
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Locher, K. P. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3216 · Cited by 804
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Mendoza, J. L., Schmidt, A., Li, Q., Nuvaga, E., Barrett, T., Bridges, R. J., Feranchak, A. P., Brautigam, C. A., & Thomas, P. J. (2012) · Cell · doi:10.1016/j.cell.2011.11.023 · Cited by 261
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Metadata
- Authors
- Dawson, R. J. P., & Locher, K. P.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2007-02-07
- Volume
- 581
- Issue
- 5
- Pages
- 935-938
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W1981893537
- Cited by
- 406
- References
- 1
- FWCI
- 18.41
- Type
- journal article
- Language
- en
- Open access
- closed
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- Dawson, R. J. P., & Locher, K. P. (2007). Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP‐PNP. FEBS Letters. https://doi.org/10.1016/j.febslet.2007.01.073
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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