Structure of the C-terminal domain of the surface antigen SpaP from the caries pathogen Streptococcus mutans

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 plaqu...

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Detalles Bibliográficos
Autores principales: Nylander, Åsa, Forsgren, Nina, Persson, Karina
Formato: Texto
Lenguaje:English
Publicado: International Union of Crystallography 2010
Materias:
Structural Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3079964/
https://www.ncbi.nlm.nih.gov/pubmed/21206016
http://dx.doi.org/10.1107/S174430911004443X
Descripción
Sumario: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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