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

Nylander, A.; Forsgren, N.; Persson, K.

Acta Crystallographica. Section F Structural Biology and Crystallization Communications 67(Part 1): 23-26

2011


ISSN/ISBN: 1744-3091
PMID: 21206016
DOI: 10.1107/s174430911004443x
Accession: 055959140

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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.