title: Evolution of a new enzyme activity from the same motif fold.
abstract: The host cell recognition protein of the Escherichia coli bacteriophage HK620 is a large homotrimeric tailspike that cleaves the O18A1 type O antigen. The crystal structure of HK620 tailspike determined in the apo and substrate-bound form is reported by Barbirz et al. in this issue of Molecular Microbiology. Lacking detectable sequence similarity, the fold and overall organization of the HK620 tailspike are similar to those of the tailspikes of the related phages P22 and Sf6. The substrate-binding site is intrasubunit in P22 and HK620 tailspikes, but intersubunit in Sf6, demonstrating how phages can adapt the same protein fold to recognize different substrates.
authors.affiliation: Department of Biological Sciences, Purdue University, 915 W. State Street, West Lafayette, IN 47907, USA. leiman@purdue.edu
authors.forename: Petr G
authors.initials: PG
authors.lastname: Leiman
authors.forename: Ian J
authors.initials: IJ
authors.lastname: Molineux
mesh_terms: D001665:Binding Sites; D003090:Coliphages / Q000737:chemistry* / Q000201:enzymology*; D004926:Escherichia coli / Q000821:virology*; D020836:Protein Structure, Quaternary; D017376:Viral Tail Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D017376:Viral Tail Proteins