Crystallographic analysis of AcrB

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2004
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Pos, Klaas Martinus
Schiefner, André
Seeger, Markus A.
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Zusammenfassung

A His-tagged derivative of the multidrug efflux pump AcrB could be crystallized in three different space groups (R3, R32 and P321). Experimental MAD-phasing maps from R32 AcrBHis crystals were obtained to a resolution of 3.5 Å. Datasets of native and substrate soaked AcrBHis crystals were collected at the Swiss Light Source X06SA beamline up to a resolution of 2.7 A+ and re¢nement of these data provided good quality electron density maps,which allowed us to complement the published AcrB structure (PDB code 1iwg). Introduction of amino acids 860-865 and 868 lacking in the 1iwg structure and deletion of a highly disordered region (amino acids 669-678) improved Rfree and average B factors in the 2.7 Å model. We could not identify signi¢cant densities indicating speci¢c antibiotic binding sites in the AcrB R32 space group datasets under the soaking conditions tested.

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Fachgebiet (DDC)
570 Biowissenschaften, Biologie
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AcrB, Multidrug resistance, Membrane protein, X-ray crystallography
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ISO 690POS, Klaas Martinus, André SCHIEFNER, Markus A. SEEGER, Kay DIEDERICHS, 2004. Crystallographic analysis of AcrB. In: FEBS Letters. 2004, 564(3), pp. 333-339. ISSN 0014-5793. Available under: doi: 10.1016/S0014-5793(04)00272-8
BibTex
@article{Pos2004Cryst-8129,
  year={2004},
  doi={10.1016/S0014-5793(04)00272-8},
  title={Crystallographic analysis of AcrB},
  number={3},
  volume={564},
  issn={0014-5793},
  journal={FEBS Letters},
  pages={333--339},
  author={Pos, Klaas Martinus and Schiefner, André and Seeger, Markus A. and Diederichs, Kay}
}
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