Structural highlights
Function
Q88G17_PSEPK
Publication Abstract from PubMed
A cluster of genes in the exoxis region of bacteriophage lambda 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.
The Solution Structures of Two Prophage Homologues of the Bacteriophage lambda Ea8.5 Protein Reveal a Newly Discovered Hybrid Homeodomain/Zinc-Finger Fold.,Kwan JJ, Smirnova E, Khazai S, Evanics F, Maxwell KL, Donaldson LW Biochemistry. 2013 May 14. PMID:23672713[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kwan JJ, Smirnova E, Khazai S, Evanics F, Maxwell KL, Donaldson LW. The Solution Structures of Two Prophage Homologues of the Bacteriophage lambda Ea8.5 Protein Reveal a Newly Discovered Hybrid Homeodomain/Zinc-Finger Fold. Biochemistry. 2013 May 14. PMID:23672713 doi:10.1021/bi400543w
