2h0d: Difference between revisions

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[[Image:2h0d.gif|left|200px]]


{{Structure
==Structure of a Bmi-1-Ring1B Polycomb group ubiquitin ligase complex==
|PDB= 2h0d |SIZE=350|CAPTION= <scene name='initialview01'>2h0d</scene>, resolution 2.50&Aring;
<StructureSection load='2h0d' size='340' side='right'caption='[[2h0d]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
<table><tr><td colspan='2'>[[2h0d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H0D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H0D FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
|GENE=  
<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>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h0d OCA], [https://pdbe.org/2h0d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h0d RCSB], [https://www.ebi.ac.uk/pdbsum/2h0d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h0d ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h0d OCA], [http://www.ebi.ac.uk/pdbsum/2h0d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2h0d RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/BMI1_HUMAN BMI1_HUMAN] Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. In the PRC1 complex, it is required to stimulate the E3 ubiquitin-protein ligase activity of RNF2/RING2.<ref>PMID:16359901</ref> <ref>PMID:16882984</ref> <ref>PMID:16714294</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h0/2h0d_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2h0d ConSurf].
<div style="clear:both"></div>


'''Structure of a Bmi-1-Ring1B Polycomb group ubiquitin ligase complex'''
==See Also==
 
*[[Polycomb complex protein|Polycomb complex protein]]
 
*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
==Overview==
== References ==
Polycomb group proteins Bmi-1 and Ring1B are core subunits of the PRC1 complex, which plays important roles in the regulation of Hox gene expression, X-chromosome inactivation, tumorigenesis, and stem cell self-renewal. The RING finger protein Ring1B is an E3 ligase that participates in the ubiquitination of lysine 119 of histone H2A, and the binding of Bmi-1 stimulates the E3 ligase activity. We have mapped the regions of Bmi-1 and Ring1B required for efficient ubiquitin transfer and determined a 2.5-A structure of the Bmi-1-Ring1B core domain complex. The structure reveals that Ring1B "hugs" Bmi-1 through extensive RING domain contacts and its N-terminal tail wraps around Bmi-1. The two regions of interaction have a synergistic effect on the E3 ligase activity. Our analyses suggest a model where the Bmi-1-Ring1B complex stabilizes the interaction between the E2 enzyme and the nucleosomal substrate to allow efficient ubiquitin transfer.
<references/>
 
__TOC__
==About this Structure==
</StructureSection>
2H0D is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H0D OCA].
 
==Reference==
Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex., Li Z, Cao R, Wang M, Myers MP, Zhang Y, Xu RM, J Biol Chem. 2006 Jul 21;281(29):20643-9. Epub 2006 May 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16714294 16714294]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Xu, R M.]]
[[Category: Xu RM]]
[[Category: chromatin]]
[[Category: histone]]
[[Category: polycomb]]
[[Category: transcription]]
[[Category: ubiquitin ligase]]
[[Category: wpigenetic]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:23:39 2008''
Retrieved from "https://proteopedia.org/2h0d"