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5trb

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(New page: ==Crystal structure of the RNF20 RING domain== <StructureSection load='5trb' size='340' side='right' caption='5trb, resolution 1.80&Aring;' scene=''> == Structural high...)
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==Crystal structure of the RNF20 RING domain==
==Crystal structure of the RNF20 RING domain==
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<StructureSection load='5trb' size='340' side='right' caption='[[5trb]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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<StructureSection load='5trb' size='340' side='right'caption='[[5trb]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5trb]] is a 1 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5dng 5dng]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TRB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TRB FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5trb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5dng 5dng]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TRB 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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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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=5trb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5trb OCA], [http://pdbe.org/5trb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5trb RCSB], [http://www.ebi.ac.uk/pdbsum/5trb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5trb ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=5trb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5trb OCA], [https://pdbe.org/5trb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5trb RCSB], [https://www.ebi.ac.uk/pdbsum/5trb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5trb ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/BRE1A_HUMAN BRE1A_HUMAN]] Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). It thereby plays a central role inb histone code and gene regulation. The RNF20/40 complex forms a H2B ubiquitin ligase complex in cooperation with the E2 enzyme UBE2A or UBE2B; reports about the cooperation with UBE2E1/UBCH are contradictory. Required for transcriptional activation of Hox genes. Recruited to the MDM2 promoter, probably by being recruited by p53/TP53, and thereby acts as a transcriptional coactivator. Mediates the polyubiquitination of isoform 2 of PA2G4 in cancer cells leading to its proteasome-mediated degradation.<ref>PMID:16307923</ref> <ref>PMID:16337599</ref> <ref>PMID:19037095</ref> <ref>PMID:19410543</ref>
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[https://www.uniprot.org/uniprot/BRE1A_HUMAN BRE1A_HUMAN] Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). It thereby plays a central role inb histone code and gene regulation. The RNF20/40 complex forms a H2B ubiquitin ligase complex in cooperation with the E2 enzyme UBE2A or UBE2B; reports about the cooperation with UBE2E1/UBCH are contradictory. Required for transcriptional activation of Hox genes. Recruited to the MDM2 promoter, probably by being recruited by p53/TP53, and thereby acts as a transcriptional coactivator. Mediates the polyubiquitination of isoform 2 of PA2G4 in cancer cells leading to its proteasome-mediated degradation.<ref>PMID:16307923</ref> <ref>PMID:16337599</ref> <ref>PMID:19037095</ref> <ref>PMID:19410543</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Monoubiquitylation of histone H2B is a post-translational mark that plays key roles in regulation of transcription and genome stability. In humans, attachment of ubiquitin to lysine 120 of histone H2B depends on the activity of the E2 ubiquitin-conjugating enzyme, Ube2B, and the really interesting new gene (RING) E3 ligases, RING finger protein (RNF) 20 and RNF40. To better understand the molecular basis of this modification, we have solved the crystal structure of the RNF20 RING domain and show that it is a homodimer that specifically interacts with the Ube2B~Ub conjugate. By mutating residues at the E3-E2 and E3-ubiquitin interfaces, we identify key contacts required for interaction of the RNF20 RING domain with the Ube2B~Ub conjugate. These mutants were used to generate a structure-based model of the RNF20-Ube2B~Ub complex that reveals differences from other RING-E2~Ub complexes, and suggests how the RNF20-Ube2B~Ub complex might interact with its nucleosomal substrate. Additionally, we show that the RING domains of RNF20 and RNF40 can form a stable heterodimer that is active. Together, our studies provide new insights into the mechanisms that regulate RNF20-mediated ubiquitin transfer from Ube2B.
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Structure and Function of the RING Domains of RNF20 and RNF40, Dimeric E3 Ligases that Monoubiquitylate Histone H2B.,Foglizzo M, Middleton AJ, Day CL J Mol Biol. 2016 Aug 25. pii: S0022-2836(16)30339-4. doi:, 10.1016/j.jmb.2016.07.025. PMID:27569044<ref>PMID:27569044</ref>
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==See Also==
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*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
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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 5trb" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Day, C L]]
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[[Category: Homo sapiens]]
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[[Category: Foglizzo, M]]
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[[Category: Large Structures]]
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[[Category: Middleton, A J]]
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[[Category: Day CL]]
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[[Category: Ligase]]
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[[Category: Foglizzo M]]
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[[Category: Middleton AJ]]

Current revision

Crystal structure of the RNF20 RING domain

PDB ID 5trb

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