Ontology highlight
ABSTRACT:
SUBMITTER: Su CC
PROVIDER: S-EPMC1636240 | biostudies-literature | 2006 Oct
REPOSITORIES: biostudies-literature
Su Chih-Chia CC Li Ming M Gu Ruoyu R Takatsuka Yumiko Y McDermott Gerry G Nikaido Hiroshi H Yu Edward W EW
Journal of bacteriology 20061001 20
We previously reported the X-ray structures of wild-type Escherichia coli AcrB, a proton motive force-dependent multidrug efflux pump, and its N109A mutant. These structures presumably reflect the resting state of AcrB, which can bind drugs. After ligand binding, a proton may bind to an acidic residue(s) in the transmembrane domain, i.e., Asp407 or Asp408, within the putative network of electrostatically interacting residues, which also include Lys940 and Thr978, and this may initiate a series o ...[more]