The Solution Structures of Two Prophage Homologues of the Bacteriophage λ Ea8.5 Protein Reveal a Newly Discovered Hybrid Homeodomain/Zinc-Finger Fold

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. col...

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Bibliographic Details
Published in:Biochemistry (Easton) 2013-05, Vol.52 (21), p.3612-3614
Main Authors: Kwan, Jamie J, Smirnova, Ekaterina, Khazai, Shahin, Evanics, Ferenc, Maxwell, Karen L, Donaldson, Logan W
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacteriophage lambda - chemistry
Coliphages - chemistry
Escherichia coli
Homeodomain Proteins - chemistry
Molecular Sequence Data
Nuclear Magnetic Resonance, Biomolecular
Prophages - chemistry
Protein Conformation
Pseudomonas Phages - chemistry
Pseudomonas putida
Sequence Homology, Amino Acid
Viral Proteins - chemistry
Zinc Fingers
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Summary: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.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi400543w