4C0Z
The N-terminal domain of the Streptococcus pyogenes pilus tip adhesin Cpa
Summary for 4C0Z
| Entry DOI | 10.2210/pdb4c0z/pdb |
| Descriptor | ANCILLARY PROTEIN 2, CHLORIDE ION, SPERMIDINE, ... (6 entities in total) |
| Functional Keywords | cell adhesion, thioester-domain, pilus |
| Biological source | STREPTOCOCCUS PYOGENES |
| Total number of polymer chains | 12 |
| Total formula weight | 300471.88 |
| Authors | Linke-Winnebeck, C.,Paterson, N.,Baker, E.N. (deposition date: 2013-08-08, release date: 2013-11-20, Last modification date: 2014-01-15) |
| Primary citation | Linke-Winnebeck, C.,Paterson, N.G.,Young, P.G.,Middleditch, M.J.,Greenwood, D.R.,Witte, G.,Baker, E.N. Structural Model for the Covalent Adhesion of the Streptococcus Pyogenes Pilus Through a Thioester Bond. J.Biol.Chem., 289:177-, 2014 Cited by PubMed Abstract: The human pathogen Streptococcus pyogenes produces pili that are essential for adhesion to host surface receptors. Cpa, the adhesin at the pilus tip, was recently shown to have a thioester-containing domain. The thioester bond is believed to be important in adhesion, implying a mechanism of covalent attachment analogous to that used by human complement factors. Here, we have characterized a second active thioester-containing domain on Cpa, the N-terminal domain of Cpa (CpaN). Expression of CpaN in Escherichia coli gave covalently linked dimers. These were shown by x-ray crystallography and mass spectrometry to comprise two CpaN molecules cross-linked by the polyamine spermidine following reaction with the thioester bonds. This cross-linked CpaN dimer provides a model for the covalent attachment of Cpa to target receptors and thus the streptococcal pilus to host cells. Similar thioester domains were identified in cell wall proteins of other Gram-positive pathogens, suggesting that thioester domains are more widely used and provide a mechanism of adhesion by covalent bonding to target molecules on host cells that mimics that used by the human complement system to eliminate pathogens. PubMed: 24220033DOI: 10.1074/JBC.M113.523761 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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