3vhs

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==Crystal structure of UBZ of human WRNIP1==
==Crystal structure of UBZ of human WRNIP1==
<StructureSection load='3vhs' size='340' side='right' caption='[[3vhs]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='3vhs' size='340' side='right' caption='[[3vhs]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vht|3vht]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vht|3vht]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">WRNIP1, WHIP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">WRNIP1, WHIP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<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=3vhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vhs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vhs RCSB], [http://www.ebi.ac.uk/pdbsum/3vhs PDBsum]</span></td></tr>
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<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=3vhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vhs OCA], [http://pdbe.org/3vhs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vhs RCSB], [http://www.ebi.ac.uk/pdbsum/3vhs PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/WRIP1_HUMAN WRIP1_HUMAN]] Functions as a modulator for initiation or reinitiation events during DNA polymerase delta-mediated DNA synthesis. Has an intrinsic ATPase activity that functions as a sensor of DNA damage or of arrested replication forks and regulates the extent of DNA synthesis.<ref>PMID:15670210</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The ubiquitin-binding zinc finger (UBZ) is a type of zinc-coordinating beta-beta-alpha fold domain found mainly in proteins involved in DNA repair and transcriptional regulation. Here we report the crystal structure of the UBZ domain of Y-family DNA polymerase (pol) eta and the crystal structure of the complex between the UBZ domain of Werner helicase-interacting protein 1 (WRNIP1) and ubiquitin, crystallized using the green fluorescent protein fusion technique. In contrast to the pol eta UBZ, which has been proposed to bind ubiquitin via its C-terminal alpha helix, ubiquitin binds to a novel surface of WRNIP1 UBZ composed of the first beta strand and the C-terminal alpha helix. In addition, we report the structure of the tandem UBZ domains of Tax1-binding protein 1 (TAX1BP1) and show that the second UBZ of TAX1BP1 binds ubiquitin, presumably in a manner similar to that of WRNIP1 UBZ. We propose that UBZ domains can be divided into at least two different types in terms of the ubiquitin-binding surfaces: the pol eta type and the WRNIP1 type. This article is protected by copyright. All rights reserved.
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A novel mode of ubiquitin recognition by the ubiquitin-binding zinc finger domain of WRNIP1.,Suzuki N, Rohaim A, Kato R, Dikic I, Wakatsuki S, Kawasaki M FEBS J. 2016 Apr 8. doi: 10.1111/febs.13734. PMID:27062441<ref>PMID:27062441</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3vhs" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 08:12, 1 June 2016

Crystal structure of UBZ of human WRNIP1

3vhs, resolution 1.90Å

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