4HOB

The crystal structure of the Zalpha domain from Cyprinid Herpes virus 3

Summary for 4HOB

• Entry DOI: 10.2210/pdb4hob/pdb
• Related: 1J75 1OYI 1QBJ
• Descriptor: Putative uncharacterized protein, SULFATE ION (3 entities in total)
• Functional Keywords: domain swapping, z-dna binding domain, dna and rna binding, dna binding protein
• Biological source: Cyprinid herpesvirus 3
• Total number of polymer chains: 4
• Total formula weight: 31972.16

Authors

Tome, A.R.,Kus, K.,de Rosa, M.,Paulo, L.M.,Figueiredo, D.,Athanasiadis, A. (deposition date: 2012-10-22, release date: 2013-09-11, Last modification date: 2023-11-08)

Primary citation

Tome, A.R.,Kus, K.,Correia, S.,Paulo, L.M.,Zacarias, S.,de Rosa, M.,Figueiredo, D.,Parkhouse, R.M.,Athanasiadis, A.
Crystal structure of a poxvirus-like zalpha domain from cyprinid herpesvirus 3
J.Virol., 87:3998-4004, 2013

PubMed Abstract: Zalpha domains are a subfamily of the winged helix-turn-helix domains sharing the unique ability to recognize CpG repeats in the left-handed Z-DNA conformation. In vertebrates, domains of this family are found exclusively in proteins that detect foreign nucleic acids and activate components of the antiviral interferon response. Moreover, poxviruses encode the Zalpha domain-containing protein E3L, a well-studied and potent inhibitor of interferon response. Here we describe a herpesvirus Zalpha-domain-containing protein (ORF112) from cyprinid herpesvirus 3. We demonstrate that ORF112 also binds CpG repeats in the left-handed conformation, and moreover, its structure at 1.75 Å reveals the Zalpha fold found in ADAR1, DAI, PKZ, and E3L. Unlike other Zalpha domains, however, ORF112 forms a dimer through a unique domain-swapping mechanism. Thus, ORF112 may be considered a new member of the Z-domain family having DNA binding properties similar to those of the poxvirus E3L inhibitor of interferon response.

PubMed: 23365431
DOI: 10.1128/JVI.03116-12

Experimental method

X-RAY DIFFRACTION (1.76 Å)