3opu

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

spinqualitylabelsall models 3opu, resolution 2.18Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3opu is a 6 chain structure with sequence from Streptococcus mutans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.181Å Ligands: CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PAC_STRMG Surface protein antigen implicated in dental caries. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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