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1sfu
From Proteopedia
(New page: 200px<br /><applet load="1sfu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sfu, resolution 2.0Å" /> '''Crystal structure of ...) |
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| - | [[Image:1sfu.gif|left|200px]]<br /><applet load="1sfu" size=" | + | [[Image:1sfu.gif|left|200px]]<br /><applet load="1sfu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1sfu, resolution 2.0Å" /> | caption="1sfu, resolution 2.0Å" /> | ||
'''Crystal structure of the viral Zalpha domain bound to left-handed Z-DNA'''<br /> | '''Crystal structure of the viral Zalpha domain bound to left-handed Z-DNA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A conserved feature of poxviruses is a protein, well characterized as E3L | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1SFU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Viruses Viruses]. Full crystallographic information is available from [http:// | + | 1SFU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Viruses Viruses]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SFU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Viruses]] | [[Category: Viruses]] | ||
| - | [[Category: Ha, S | + | [[Category: Ha, S C.]] |
| - | [[Category: Kim, K | + | [[Category: Kim, K K.]] |
| - | [[Category: Kim, Y | + | [[Category: Kim, Y G.]] |
[[Category: Lowenhaupt, K.]] | [[Category: Lowenhaupt, K.]] | ||
| - | [[Category: Quyen, D | + | [[Category: Quyen, D Van.]] |
[[Category: Rich, A.]] | [[Category: Rich, A.]] | ||
| - | [[Category: Wu, C | + | [[Category: Wu, C A.]] |
[[Category: protein/z-dna complex]] | [[Category: protein/z-dna complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:01:07 2008'' |
Revision as of 13:01, 21 February 2008
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Crystal structure of the viral Zalpha domain bound to left-handed Z-DNA
Overview
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.
About this Structure
1SFU is a Single protein structure of sequence from Viruses. Full crystallographic information is available from OCA.
Reference
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
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