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1oyi
From Proteopedia
(Difference between revisions)
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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 | + | <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=' | + | </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. | ||
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| - | 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®/PubMed®, 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 | + | [[Category: Kahmann JD]] |
| - | [[Category: Kim | + | [[Category: Kim Y-G]] |
| - | [[Category: Lowenhaupt | + | [[Category: Lowenhaupt K]] |
| - | [[Category: Oschkinat | + | [[Category: Oschkinat H]] |
| - | [[Category: Putter | + | [[Category: Putter V]] |
| - | [[Category: Rich | + | [[Category: Rich A]] |
| - | [[Category: Schade | + | [[Category: Schade M]] |
| - | [[Category: Schmieder | + | [[Category: Schmieder P]] |
| - | [[Category: Wecking | + | [[Category: Wecking DA]] |
| - | + | ||
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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Categories: Large Structures | Vaccinia virus | Kahmann JD | Kim Y-G | Lowenhaupt K | Oschkinat H | Putter V | Rich A | Schade M | Schmieder P | Wecking DA
