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Updated: Jun 5, 2026

Purification of a High Molecular Mass Protein in Streptococcus mutans
Published on: September 14, 2019
Structure of the C-terminal domain of the surface antigen SpaP from the caries pathogen Streptococcus mutans
Asa Nylander1, Nina Forsgren, Karina Persson
1Department of Odontology, Umeå University, SE-901 87 Umeå, Sweden.
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.
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