3OPU

Crystal structure of the C-terminal domain of Streptococcus mutans surface protein SpaP

Summary for 3OPU

• Entry DOI: 10.2210/pdb3opu/pdb
• Descriptor: SpaP, CALCIUM ION (3 entities in total)
• Functional Keywords: cell adhesion
• Biological source: Streptococcus mutans
• Total number of polymer chains: 6
• Total formula weight: 228433.33

Authors

Nylander, A.,Persson, K. (deposition date: 2010-09-02, release date: 2011-01-19, Last modification date: 2024-10-16)

Primary citation

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, 67:23-26, 2011

PubMed 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.

PubMed: 21206016
DOI: 10.1107/S174430911004443X

Experimental method

X-RAY DIFFRACTION (2.181 Å)