New insights into the glycosylation of the surface layer protein SgsE from Geobacillus stearothermophilus NRS 2004/3a.

@article{Steiner2006NewII,
  title={New insights into the glycosylation of the surface layer protein SgsE from Geobacillus stearothermophilus NRS 2004/3a.},
  author={Kerstin Steiner and Gottfried Pohlentz and Klaus Dreisewerd and Stefan Berkenkamp and Paul Messner and Jasna Peter-Katalini{\'c} and Christina Sch{\"a}ffer},
  journal={Journal of bacteriology},
  year={2006},
  volume={188 22},
  pages={7914-21}
}
The surface of Geobacillus stearothermophilus NRS 2004/3a cells is covered by an oblique surface layer (S-layer) composed of glycoprotein subunits. To this S-layer glycoprotein, elongated glycan chains are attached that are composed of [-->2)-alpha-l-Rhap-(1-->3)-beta-l-Rhap-(1-->2)-alpha-L-Rhap-(1-->] repeating units, with a 2-O-methyl modification of the terminal trisaccharide at the nonreducing end of the glycan chain and a core saccharide as linker to the S-layer protein. On sodium dodecyl… CONTINUE READING

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