4r7e

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'''Unreleased structure'''
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==Structure of Bre1 RING domain==
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<StructureSection load='4r7e' size='340' side='right' caption='[[4r7e]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4r7e]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R7E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R7E FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4r7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r7e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r7e RCSB], [http://www.ebi.ac.uk/pdbsum/4r7e PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/BRE1_YEAST BRE1_YEAST]] E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H2B to form H2BK123ub1 in association with the E2 enzyme RAD6/UBC2. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. It thereby plays a central role in histone code and gene regulation. Also modulates the formation of double-strand breaks during meiosis.<ref>PMID:12535538</ref> <ref>PMID:12535539</ref> <ref>PMID:12876294</ref> <ref>PMID:15280549</ref> <ref>PMID:15632065</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Monoubiquitination of histone H2B at Lys123 in yeast plays a critical role in regulating transcription, mRNA export, DNA replication, and the DNA damage response. The RING E3 ligase, Bre1, catalyzes monoubiquitination of H2B in concert with the E2 ubiquitin-conjugating enzyme, Rad6. The crystal structure of a C-terminal fragment of Bre1 shows that the catalytic RING domain is preceded by an N-terminal helix that mediates coiled-coil interactions with a crystallographically related monomer. Homology modeling suggests that the human homologue of Bre1, RNF20/RNF40, heterodimerizes through similar coiled-coil interactions. Proteins 2015;. (c) 2015 The Authors. Proteins: Structure, Function, and Bioinformatics Published by Wiley Periodicals, Inc.
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The entry 4r7e is ON HOLD until Paper Publication
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Structure of the yeast Bre1 RING domain.,Kumar P, Wolberger C Proteins. 2015 Apr 9. doi: 10.1002/prot.24812. PMID:25864391<ref>PMID:25864391</ref>
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Authors: Kumar, P., Wolberger, C.
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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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Description: Structure of Bre1 RING domain
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Kumar, P]]
[[Category: Wolberger, C]]
[[Category: Wolberger, C]]
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[[Category: Kumar, P]]
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[[Category: E3 ubiquitin ligase]]
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[[Category: Ligase]]
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[[Category: Monoubiquitination of histone h2b at k123]]
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[[Category: Nucleosome]]
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[[Category: Nucleus]]
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[[Category: Rad6]]
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[[Category: Zinc finger domain]]

Revision as of 12:17, 13 May 2015

Structure of Bre1 RING domain

4r7e, resolution 2.25Å

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