1SFU

Crystal structure of the viral Zalpha domain bound to left-handed Z-DNA

Summary for 1SFU

• Entry DOI: 10.2210/pdb1sfu/pdb
• Descriptor: 5'-D(*T*CP*GP*CP*GP*CP*G)-3', 34L protein (3 entities in total)
• Functional Keywords: protein-z-dna complex, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Yaba-like disease virus
• Total number of polymer chains: 4
• Total formula weight: 21673.07

Authors

Ha, S.C.,Van Quyen, D.,Wu, C.A.,Lowenhaupt, K.,Rich, A.,Kim, Y.G.,Kim, K.K. (deposition date: 2004-02-20, release date: 2004-08-17, Last modification date: 2024-02-14)

Primary citation

Ha, S.C.,Lokanath, N.K.,Van Quyen, D.,Wu, C.A.,Lowenhaupt, K.,Rich, A.,Kim, Y.G.,Kim, K.K.
A poxvirus protein forms a complex with left-handed Z-DNA: crystal structure of a Yatapoxvirus Zalpha bound to DNA.
Proc.Natl.Acad.Sci.USA, 101:14367-14372, 2004

PubMed Abstract: A conserved feature of poxviruses is a protein, well characterized as E3L in vaccinia virus, that confers IFN resistance on the virus. This protein comprises two domains, an N-terminal Z-DNA-binding protein domain (Zalpha) and a C-terminal double-stranded RNA-binding domain. Both are required for pathogenicity of vaccinia virus in mice infected by intracranial injection. Here, we describe the crystal structure of the Zalpha domain from the E3L-like protein of Yaba-like disease virus, a Yatapoxvirus, in a complex with Z-DNA, solved at a 2.0-A resolution. The DNA contacting surface of Yaba-like disease virus Zalpha(E3L) closely resembles that of other structurally defined members of the Zalpha family, although some variability exists in the beta-hairpin region. In contrast to the Z-DNA-contacting surface, the nonbinding surface of members of the Zalpha family are unrelated; this surface may effect protein-specific interactions. The presence of the conserved and tailored Z-DNA-binding surface, which interacts specifically with the zigzag backbone and syn base diagnostic of the Z-form, reinforces the importance to poxvirus infection of the ability of this protein to recognize the Z-conformation.

PubMed: 15448208
DOI: 10.1073/pnas.0405586101

Experimental method

X-RAY DIFFRACTION (2 Å)