Structural highlights
Publication Abstract from PubMed
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 A 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.
Structure of the C-terminal domain of the surface antigen SpaP from the caries pathogen Streptococcus mutans.,Nylander A, Forsgren N, Persson K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jan 1;67(Pt, 1):23-6. Epub 2010 Dec 21. PMID:21206016[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nylander A, Forsgren N, Persson K. Structure of the C-terminal domain of the surface antigen SpaP from the caries pathogen Streptococcus mutans. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jan 1;67(Pt, 1):23-6. Epub 2010 Dec 21. PMID:21206016 doi:10.1107/S174430911004443X
