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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.

SUBMITTER: Nylander A

PROVIDER: S-EPMC3079964 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

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

Nylander Asa A Forsgren Nina N Persson Karina K

Acta crystallographica. Section F, Structural biology and crystallization communications 20101221 Pt 1

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 ...[more]

PMID: 21206016

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