1sfu

<StructureSection load='1sfu' size='340' side='right' caption='[[1sfu]], [[Resolution|resolution]] 2.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[1sfu]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Tanapox_virus_strain_davis Tanapox virus strain davis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SFU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SFU FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sfu OCA], [http://pdbe.org/1sfu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sfu RCSB], [http://www.ebi.ac.uk/pdbsum/1sfu PDBsum]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sf/1sfu_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

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.

A poxvirus protein forms a complex with left-handed Z-DNA: crystal structure of a Yatapoxvirus Zalpha bound to DNA.,Ha SC, Lokanath NK, Van Quyen D, Wu CA, Lowenhaupt K, Rich A, Kim YG, Kim KK Proc Natl Acad Sci U S A. 2004 Oct 5;101(40):14367-72. Epub 2004 Sep 24. PMID:15448208<ref>PMID:15448208</ref>

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== References ==

[[Category: Tanapox virus strain davis]]

[[Category: Ha, S C]]

[[Category: Kim, K K]]

[[Category: Kim, Y G]]

[[Category: Lowenhaupt, K]]

[[Category: Quyen, D Van]]

[[Category: Rich, A]]

[[Category: Wu, C A]]

[[Category: Dna binding protein-dna complex]]

[[Category: Protein-z-dna complex]]