Crystal structure of the NanB sialidase from Streptococcus pneumoniae.

@article{Xu2008CrystalSO,
  title={Crystal structure of the NanB sialidase from Streptococcus pneumoniae.},
  author={Guogang Xu and Jane A. Potter and Rupert J. M. Russell and Marco R Oggioni and P. W. Andrew and Garry L. Taylor},
  journal={Journal of molecular biology},
  year={2008},
  volume={384 2},
  pages={436-49}
}
The Streptococcus pneumoniae genomes encode up to three sialidases (or neuraminidases), NanA, NanB and NanC, which are believed to be involved in removing sialic acid from host cell surface glycans, thereby promoting colonization of the upper respiratory tract. Here, we present the crystal structure of NanB to 1.7 A resolution derived from a crystal grown in the presence of the buffer Ches (2-N-cyclohexylaminoethanesulfonic acid). Serendipitously, Ches was found bound to NanB at the enzyme… CONTINUE READING
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