2XIC

Pilus-presented adhesin, Spy0125 (Cpa), P212121 form (ESRF data)

2XIC の概要

• エントリーDOI: 10.2210/pdb2xic/pdb
• 分子名称: ANCILLARY PROTEIN 1 (2 entities in total)
• 機能のキーワード: cell adhesion, gram positive pilus, adhesin, intramolecular isopeptide bond, internal thioester
• 由来する生物種: STREPTOCOCCUS PYOGENES
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 102950.87

構造登録者

Pointon, J.A.,Smith, W.D.,Saalbach, G.,Crow, A.,Kehoe, M.A.,Banfield, M.J. (登録日: 2010-06-28, 公開日: 2010-08-04, 最終更新日: 2024-10-23)

主引用文献

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 is Required for Efficient Host Cell Interaction
J.Biol.Chem., 285:33858-, 2010

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: 20729215
DOI: 10.1074/JBC.M110.149385

実験手法

X-RAY DIFFRACTION (2.9 Å)