Crystal structure and enantiomer selection by D-alanyl carrier protein ligase DltA from Bacillus cereus.

@article{Du2008CrystalSA,
  title={Crystal structure and enantiomer selection by D-alanyl carrier protein ligase DltA from Bacillus cereus.},
  author={Liqin Du and Yujiong He and Yu Bing Luo},
  journal={Biochemistry},
  year={2008},
  volume={47 44},
  pages={11473-80}
}
Ubiquitous D-alanylation of lipoteichoic acids modulates the surface charge and ligand binding of the gram-positive cell wall. Disruption of the bacterial DltABCD gene involved in teichoic acid alanylation, as well as inhibition of the DltA protein, has been shown to increase a gram-positive bacterium's susceptibility to antibiotics. The DltA D-alanyl carrier protein ligase promotes a two-step process starting with adenylation of D-alanine. We have determined the 2.0 A resolution crystal… CONTINUE READING
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