Crystal structure of the multidrug efflux transporter AcrB at 3.1A resolution reveals the N-terminal region with conserved amino acids.

@article{Das2007CrystalSO,
  title={Crystal structure of the multidrug efflux transporter AcrB at 3.1A resolution reveals the N-terminal region with conserved amino acids.},
  author={Debanu Das and Qian Steven Xu and Jonas Yun Lee and Irina V Ankoudinova and Candice Huang and Yun Lou and A. Degiovanni and Rosalind Kim and Sung-Hou Kim},
  journal={Journal of structural biology},
  year={2007},
  volume={158 3},
  pages={494-502}
}
Crystal structures of the bacterial multidrug transporter AcrB in R32 and C2 space groups showing both symmetric and asymmetric trimeric assemblies, respectively, supplemented with biochemical investigations, have provided most of the structural basis for a molecular level understanding of the protein structure and mechanisms for substrate uptake and translocation carried out by this 114-kDa inner membrane protein. They suggest that AcrB captures ligands primarily from the periplasm. Substrates… CONTINUE READING

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