Protein Domain : P22 tailspike C-terminal domain IPR015331

Type	Domain
Description	The tailspike protein of Salmonella bacteriophage P22 is a viral adhesion protein that mediates attachment of the viral protein to host cell-surface lipopolysaccharide. The tailspike protein displays both receptor binding and destroying properties, inactivating the receptor by endoglycosidase activity. P22 tailspike is a homotrimer composed of 666 amino acid polypeptide chains. P22 tailspike consists of three main structural elements: the head-binding domain at the N terminus, the β-helix in the centre of the protein, and the β-prism and caudal fin at the C terminus [ ]. The P22 tailspike protein contains similar structural elements to pectin lyase []. The binding of the disaccharide product occurs within a positively charged cleft formed by loops extending from the surface of the β-helix structure. Amino acid residues responsible for recognition of the disaccharide, as well as potential catalytic residues, have been identified [].This entry represents the C-terminal domain of the tailspike protein.
Short Name	P22_tailspike_C