Crystal structure of an efficacious gonococcal adherence inhibitor: An enolase from Lactobacillus gasseri

@article{Raghunathan2014CrystalSO,
  title={Crystal structure of an efficacious gonococcal adherence inhibitor: An enolase from Lactobacillus gasseri},
  author={Kannan Raghunathan and Paul T. Harris and Rachel R. Spurbeck and Cindy Grove Arvidson and Dennis N. Arvidson},
  journal={FEBS Letters},
  year={2014},
  volume={588}
}
Enolases are highly conserved metalloenzymes ubiquitous to cellular metabolism. While these enzymes share a large degree of sequence and structural similarity, they have been shown to possess a wide range of moonlighting functions. Recent studies showed that an enolase from Lactobacillus gasseri impedes the ability of Neisseria gonorrhoeae to adhere to epithelial cells. We present the crystal structure of this enolase, the first from Lactobacillus, with one of its Mg2+ cofactors. Determined… Expand
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