crystal structure of escherichia coli phage hk620 tailspike: podoviral tailspike endoglycosidase modules are evolutionarily related.bacteriophage hk620 infects escherichia coli h and is closely related to shigella phage sf6 and salmonella phage p22. all three podoviridae recognize and cleave their respective host cell receptor polysaccharide by homotrimeric tailspike proteins. the three proteins exhibit high sequence identity in the 110 residues of their n-terminal particle-binding domains, but no apparent sequence similarity in their major, receptor-binding parts. we have biochemically characterized the receptor-binding par ...200818547389
evolution of a new enzyme activity from the same motif fold.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-bindi ...200818433454
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