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Evolution of a new enzyme activity from the same motif fold
Author(s) -
Leiman Petr G.,
Molineux Ian J.
Publication year - 2008
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2008.06241.x
Subject(s) - biology , bacteriophage , escherichia coli , peptide sequence , enzyme , computational biology , biochemistry , gene
Summary 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 intra subunit in P22 and HK620 tailspikes, but inter subunit in Sf6, demonstrating how phages can adapt the same protein fold to recognize different substrates.