The solution structures of two prophage homologues of the bacteriophage λ Ea8.5 protein reveal a newly discovered hybrid homeodomain/zinc-finger fold

Biochemistry. 2013 May 28;52(21):3612-4. doi: 10.1021/bi400543w. Epub 2013 May 14.

Abstract

A cluster of genes in the exoxis region of bacteriophage λ are capable of inhibiting the initiation of DNA synthesis in Escherichia coli. The most indispensible gene in this region is ea8.5. Here, we report the nuclear magnetic resonance structures of two ea8.5 orthologs from enteropathogenic E. coli and Pseudomonas putida prophages. Both proteins are characterized by a fused homeodomain/zinc-finger fold that escaped detection by primary sequence search methods. While these folds are both associated with a nucleic acid binding function, the amino acid composition suggests otherwise, leading to the possibility that Ea8.5 associates with other viral and host proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacteriophage lambda / chemistry*
  • Coliphages / chemistry
  • Homeodomain Proteins / chemistry*
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Prophages / chemistry*
  • Protein Conformation
  • Pseudomonas Phages / chemistry
  • Sequence Homology, Amino Acid
  • Viral Proteins / chemistry*
  • Zinc Fingers*

Substances

  • Homeodomain Proteins
  • Viral Proteins

Associated data

  • PDB/2M7A
  • PDB/2M7B