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==Solution structure of the Z-DNA binding domain of the vaccinia virus gene E3L==
==Solution structure of the Z-DNA binding domain of the vaccinia virus gene E3L==
<StructureSection load='1oyi' size='340' side='right'caption='[[1oyi]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='1oyi' size='340' side='right'caption='[[1oyi]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1oyi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OYI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OYI FirstGlance]. <br>
<table><tr><td colspan='2'>[[1oyi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OYI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OYI FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">E3L ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10245 Vaccinia virus])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oyi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oyi OCA], [https://pdbe.org/1oyi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oyi RCSB], [https://www.ebi.ac.uk/pdbsum/1oyi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oyi ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oyi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oyi OCA], [https://pdbe.org/1oyi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oyi RCSB], [https://www.ebi.ac.uk/pdbsum/1oyi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oyi ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q86638_9POXV Q86638_9POXV]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1oyi ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1oyi ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The N-terminal domain of the vaccinia virus protein E3L (Z alpha(E3L)) is essential for full viral pathogenicity in mice. It has sequence similarity to the high-affinity human Z-DNA-binding domains Z alpha(ADAR1) and Z alpha(DLM1). Here, we report the solution structure of Z alpha(E3L) and the chemical shift map of its interaction surface with Z-DNA. The global structure and the Z-DNA interaction surface of Z alpha(E3L) are very similar to the high-affinity Z-DNA-binding domains Z alpha(ADAR1) and Z alpha(DLM1). However, the key Z-DNA contacting residue Y48 of Z alpha(E3L) adopts a different side chain conformation in unbound Z alpha(E3L), which requires rearrangement for binding to Z-DNA. This difference suggests a molecular basis for the significantly lower in vitro affinity of Z alpha(E3L) to Z-DNA compared with its homologues.
The solution structure of the N-terminal domain of E3L shows a tyrosine conformation that may explain its reduced affinity to Z-DNA in vitro.,Kahmann JD, Wecking DA, Putter V, Lowenhaupt K, Kim YG, Schmieder P, Oschkinat H, Rich A, Schade M Proc Natl Acad Sci U S A. 2004 Mar 2;101(9):2712-7. Epub 2004 Feb 23. PMID:14981270<ref>PMID:14981270</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1oyi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Vaccinia virus]]
[[Category: Vaccinia virus]]
[[Category: Kahmann, J D]]
[[Category: Kahmann JD]]
[[Category: Kim, Y G]]
[[Category: Kim Y-G]]
[[Category: Lowenhaupt, K]]
[[Category: Lowenhaupt K]]
[[Category: Oschkinat, H]]
[[Category: Oschkinat H]]
[[Category: Putter, V]]
[[Category: Putter V]]
[[Category: Rich, A]]
[[Category: Rich A]]
[[Category: Schade, M]]
[[Category: Schade M]]
[[Category: Schmieder, P]]
[[Category: Schmieder P]]
[[Category: Wecking, D A]]
[[Category: Wecking DA]]
[[Category: Viral protein]]

Revision as of 05:51, 17 April 2024

Solution structure of the Z-DNA binding domain of the vaccinia virus gene E3L

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