A crystallizable form of theStreptococcus gordoniisurface antigen SspB C-domain obtained by limited proteolysis
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A crystallizable form of the Streptococcus gordonii surface antigen SspB C-domain obtained by limited proteolysis.
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 id...
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The ssrA-degradation tag sequence contains contiguous binding sites for the SspB adaptor and the ClpX component of the ClpXP protease. Although SspB normally enhances ClpXP degradation of ssrA-tagged substrates, it inhibits proteolysis under conditions that prevent tethering to ClpX. By increasing the spacing between the protease and adaptor-binding determinants in the ssrA tag, substrates were...
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Limited proteolysis experiments can be successfully used to probe conformational features of proteins. In a number of studies it has been demonstrated that the sites of limited proteolysis along the polypeptide chain of a protein are characterized by enhanced backbone flexibility, implying that proteolytic probes can pinpoint the sites of local unfolding in a protein chain. Limited proteolysis ...
متن کاملprobing conformational feature of a recombinant pyruvate kinase by limited proteolysis
pyruvate kinase is a key enzyme in glycolytic pathway that catalyzes the transphosphorylation between phosphoenolpyruvate and adp to yield atp and pyruvate. geobacillus stearothermophillus has a stable pyruvate kinase with determined crystal structure that composed of four separate domains. given that limited proteolysis experiments can be successfully used to probe conformational features of p...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section F Structural Biology and Crystallization Communications
سال: 2009
ISSN: 1744-3091
DOI: 10.1107/s1744309109021046