4OFQ

Structure of the C-terminal domain of the Streptococcus pyogenes antigen I/II-family protein AspA

Summary for 4OFQ

• Entry DOI: 10.2210/pdb4ofq/pdb
• Descriptor: Putative cell surface protein, CALCIUM ION (3 entities in total)
• Functional Keywords: beta sandwich, adhesin, cell surface, cell adhesion
• Biological source: Streptococcus pyogenes
• Total number of polymer chains: 2
• Total formula weight: 77979.53

Authors

Hall, M.,Nylander, A.,Jenkinson, H.F.,Persson, K. (deposition date: 2014-01-15, release date: 2014-03-12, Last modification date: 2024-11-27)

Primary citation

Hall, M.,Nylander, S.,Jenkinson, H.F.,Persson, K.
Structure of the C-terminal domain of AspA (antigen I/II-family) protein from Streptococcus pyogenes.
FEBS Open Bio, 4:283-289, 2014

PubMed Abstract: The pathogenic bacteria Streptococcus pyogenes can cause an array of diseases in humans, including moderate infections such as pharyngitis (strep throat) as well as life threatening conditions such as necrotizing fasciitis and puerperal fever. The antigen I/II family proteins are cell wall anchored adhesin proteins found on the surfaces of most oral streptococci and are involved in host colonization and biofilm formation. In the present study we have determined the crystal structure of the C2-3-domain of the antigen I/II type protein AspA from S. pyogenes M type 28. The structure was solved to 1.8 Å resolution and shows that the C2-3-domain is comprised of two structurally similar DEv-IgG motifs, designated C2 and C3, both containing a stabilizing covalent isopeptide bond. Furthermore a metal binding site is identified, containing a bound calcium ion. Despite relatively low sequence identity, interestingly, the overall structure shares high similarity to the C2-3-domains of antigen I/II proteins from Streptococcus gordonii and Streptococcus mutans, although certain parts of the structure exhibit distinct features. In summary this work constitutes the first step in the full structure determination of the AspA protein from S. pyogenes.

PubMed: 24918040
DOI: 10.1016/j.fob.2014.02.012

Experimental method

X-RAY DIFFRACTION (1.8 Å)