title: Structure of the C-terminal domain of the surface antigen SpaP from the caries pathogen Streptococcus mutans.
abstract: SpaP is a 1500-residue adhesin expressed on the surface of the caries-implicated bacterium Streptococcus mutans. SpaP is a member of the antigen I/II (AgI/II) family of proteins expressed by oral streptococci. These surface proteins are crucial for the incorporation of streptococci into dental plaque. The structure of the C-terminal domain of SpaP (residues 1136-1489) was solved and refined to 2.2 Å resolution with six molecules in the asymmetric unit. Similar to a related AgI/II structure, SpaP is stabilized by isopeptide bonds between lysine and asparagine side chains.
authors.affiliation: Department of Odontology, Umeå University, SE-901 87 Umeå, Sweden.
authors.forename: Asa
authors.initials: A
authors.lastname: Nylander
authors.forename: Nina
authors.initials: N
authors.lastname: Forsgren
authors.forename: Karina
authors.initials: K
authors.lastname: Persson
mesh_terms: D018829:Adhesins, Bacterial / Q000737:chemistry*; D000942:Antigens, Bacterial / Q000737:chemistry*; D000954:Antigens, Surface; D002118:Calcium / Q000737:chemistry; D018360:Crystallography, X-Ray; D003731:Dental Caries / Q000382:microbiology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D013295:Streptococcus mutans / Q000737:chemistry*
chemical_list: D018829:Adhesins, Bacterial; D000942:Antigens, Bacterial; D000954:Antigens, Surface; D002118:Calcium