A crystallizable form of the Streptococcus gordonii surface antigen SspB C-domain obtained by limited proteolysis.
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ABSTRACT:
SUBMITTER: Forsgren N
PROVIDER: S-EPMC2705642 | biostudies-literature | 2009 Jul
REPOSITORIES: biostudies-literature
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A crystallizable form of the Streptococcus gordonii surface antigen SspB C-domain obtained by limited proteolysis.
Forsgren Nina N Lamont Richard J RJ Persson Karina K
Acta crystallographica. Section F, Structural biology and crystallization communications 20090627 Pt 7
SspB is a 1500-residue adhesin expressed on the surface of the oral bacterium Streptococcus gordonii. Its interaction with other bacteria and host cells initiates the development of dental plaque. The full-length C-terminal domain of SspB was cloned, overexpressed in Escherichia coli and purified. However, the protein could not be crystallized. Limited proteolysis of the full-length C-domain identified a core fragment. The proteolysis product was cloned, expressed and purified. The protein was c ...[more]
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