2XID
Pilus-presented adhesin, Spy0125 (Cpa), P212121 form (DLS)
Summary for 2XID
| Entry DOI | 10.2210/pdb2xid/pdb |
| Related | 2XI9 2XIC |
| Descriptor | ANCILLARY PROTEIN 1 (2 entities in total) |
| Functional Keywords | cell adhesion, gram positive pilus, adhesin, intramolecular isopeptide bond, internal thioester |
| Biological source | STREPTOCOCCUS PYOGENES |
| Total number of polymer chains | 2 |
| Total formula weight | 102575.71 |
| Authors | Pointon, J.A.,Smith, W.D.,Saalbach, G.,Crow, A.,Kehoe, M.A.,Banfield, M.J. (deposition date: 2010-06-28, release date: 2010-08-04, Last modification date: 2024-10-23) |
| Primary citation | Pointon, J.A.,Smith, W.D.,Saalbach, G.,Crow, A.,Kehoe, M.A.,Banfield, M.J. A Highly Unusual Thioester Bond in a Pilus Adhesin Required for Efficient Host Cell Interaction J.Biol.Chem., 285:33858-, 2010 Cited by PubMed Abstract: Many bacterial pathogens present adhesins at the tips of long macromolecular filaments known as pili that are often important virulence determinants. Very little is known about how pili presented by Gram-positive pathogens mediate host cell binding. The crystal structure of a pilus adhesin from the important human pathogen Streptococcus pyogenes reveals an internal thioester bond formed between the side chains of a cysteine and a glutamine residue. The presence of the thioester was verified using UV-visible spectroscopy and mass spectrometry. This unusual bond has only previously been observed in thioester domains of complement and complement-like proteins where it is used to form covalent attachment to target molecules. The structure also reveals two intramolecular isopeptide bonds, one of these formed through a Lys/Asp residue pair, which are strategically positioned to confer protein stability. Removal of the internal thioester by allele-replacement mutagenesis in S. pyogenes severely compromises bacterial adhesion to model host cells. Although current paradigms of bacterial/host cell interaction envisage strong non-covalent interactions, the present study suggests cell adhesion could also involve covalent bonds. PubMed: 20729215DOI: 10.1074/JBC.M110.149385 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.65 Å) |
Structure validation
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