Evolution of a new enzyme activity from the same motif fold

Petr Leiman, Ian J. Molineux

Research output: Contribution to journalComment/debate

24 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)287-290
Number of pages4
JournalMolecular Microbiology
Volume69
Issue number2
DOIs
StatePublished - Jul 2008
Externally publishedYes

Fingerprint

Bacteriophages
Bacteriophage P22
O Antigens
Escherichia coli Proteins
Enzymes
Microbiology
Binding Sites
Proteins

ASJC Scopus subject areas

  • Molecular Biology
  • Microbiology

Cite this

Evolution of a new enzyme activity from the same motif fold. / Leiman, Petr; Molineux, Ian J.

In: Molecular Microbiology, Vol. 69, No. 2, 07.2008, p. 287-290.

Research output: Contribution to journalComment/debate

Leiman, Petr ; Molineux, Ian J. / Evolution of a new enzyme activity from the same motif fold. In: Molecular Microbiology. 2008 ; Vol. 69, No. 2. pp. 287-290.
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