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 identified a core fragment. The proteolysis product was cloned, expressed and purified. The protein was crystallized using the hanging-drop vapour-diffusion method. X-ray data were collected and processed to a maximum resolution of 2.1 A with 96.4% completeness. The crystals belonged to space group P2(1), with one molecule in the asymmetric unit, a solvent content of 33.7% and a corresponding Matthews coefficient of 1.85 A(3) Da(-1).
Forsgren
Nina
N
Department of Odontology, Umeå University, Umeå SE-90 187, Sweden.
Lamont
Richard J
RJ
Persson
Karina
K
D018829:Adhesins, Bacterial / Q000737:chemistry*; D000942:Antigens, Bacterial / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D050505:Mutant Proteins / Q000737:chemistry; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D054773:Streptococcus gordonii / Q000737:chemistry*
D018829:Adhesins, Bacterial; D000942:Antigens, Bacterial; D050505:Mutant Proteins; C068465:salivary agglutinin receptor, Streptocococcus