Conservation of structure and mechanism in primary and secondary transporters exemplified by SiaP, a sialic acid binding virulence factor from Haemophilus influenzae.

@article{Mller2006ConservationOS,
  title={Conservation of structure and mechanism in primary and secondary transporters exemplified by SiaP, a sialic acid binding virulence factor from Haemophilus influenzae.},
  author={Axel R. Von M{\"u}ller and Emmanuele Severi and Christopher Mulligan and Andrew G. Watts and David J. Kelly and Keith S Wilson and Anthony James Wilkinson and Gavin H Thomas},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 31},
  pages={
          22212-22
        }
}
Extracytoplasmic solute receptors (ESRs) are important components of solute uptake systems in bacteria, having been studied extensively as parts of ATP binding cassette transporters. Herein we report the first crystal structure of an ESR protein from a functionally characterized electrochemical ion gradient dependent secondary transporter. This protein, SiaP, forms part of a tripartite ATP-independent periplasmic transporter specific for sialic acid in Haemophilus influenzae. Surprisingly, the… CONTINUE READING

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