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| | <StructureSection load='1pk1' size='340' side='right'caption='[[1pk1]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='1pk1' size='340' side='right'caption='[[1pk1]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1pk1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PK1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PK1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1pk1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PK1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PK1 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1pk3|1pk3]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PH-P ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), Sex Comb on Midleg ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=1pk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pk1 OCA], [https://pdbe.org/1pk1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pk1 RCSB], [https://www.ebi.ac.uk/pdbsum/1pk1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pk1 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=1pk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pk1 OCA], [https://pdbe.org/1pk1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pk1 RCSB], [https://www.ebi.ac.uk/pdbsum/1pk1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pk1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PHP_DROME PHP_DROME]] Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. Component of the PcG multiprotein PRC1 complex, a complex that acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-118', rendering chromatin heritably changed in its expressibility. Plays a role in regulating the expression of other pair-rule genes such as eve, ftz, and H.<ref>PMID:1346609</ref> [[https://www.uniprot.org/uniprot/SCM_DROME SCM_DROME]] Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They probably act via the methylation of histones, rendering chromatin heritably changed in its expressibility.<ref>PMID:15280237</ref> [UniProtKB:Q9W3C1]
| + | [https://www.uniprot.org/uniprot/PHP_DROME PHP_DROME] Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. Component of the PcG multiprotein PRC1 complex, a complex that acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-118', rendering chromatin heritably changed in its expressibility. Plays a role in regulating the expression of other pair-rule genes such as eve, ftz, and H.<ref>PMID:1346609</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pk/1pk1_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pk/1pk1_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bowie, J U]] | + | [[Category: Bowie JU]] |
| - | [[Category: Cascio, D]] | + | [[Category: Cascio D]] |
| - | [[Category: Kim, C A]] | + | [[Category: Kim CA]] |
| - | [[Category: Kim, W]] | + | [[Category: Kim W]] |
| - | [[Category: Sawaya, M R]] | + | [[Category: Sawaya MR]] |
| - | [[Category: Hetero sam domain]]
| + | |
| - | [[Category: Polymer]]
| + | |
| - | [[Category: Transcription repression]]
| + | |
| - | [[Category: Transcriptional repression]]
| + | |
| Structural highlights
Function
PHP_DROME Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. Component of the PcG multiprotein PRC1 complex, a complex that acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-118', rendering chromatin heritably changed in its expressibility. Plays a role in regulating the expression of other pair-rule genes such as eve, ftz, and H.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The polycomb group proteins are required for the stable maintenance of gene repression patterns established during development. They function as part of large multiprotein complexes created via a multitude of protein-protein interaction domains. Here we examine the interaction between the SAM domains of the polycomb group proteins polyhomeotic (Ph) and Sex-comb-on-midleg (Scm). Previously we showed that Ph-SAM polymerizes as a helical structure. We find that Scm-SAM also polymerizes, and a crystal structure reveals an architecture similar to the Ph-SAM polymer. These results suggest that Ph-SAM and Scm-SAM form a copolymer. Binding affinity measurements between Scm-SAM and Ph-SAM subunits in different orientations indicate a preference for the formation of a single junction copolymer. To provide a model of the copolymer, we determined the structure of the Ph-SAM/Scm-SAM junction. Similar binding modes are observed in both homo- and heterocomplex formation with minimal change in helix axis direction at the polymer joint. The copolymer model suggests that polymeric Scm complexes could extend beyond the local domains of polymeric Ph complexes on chromatin, possibly playing a role in long range repression.
Structural organization of a Sex-comb-on-midleg/polyhomeotic copolymer.,Kim CA, Sawaya MR, Cascio D, Kim W, Bowie JU J Biol Chem. 2005 Jul 29;280(30):27769-75. Epub 2005 May 19. PMID:15905166[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ DeCamillis M, Cheng NS, Pierre D, Brock HW. The polyhomeotic gene of Drosophila encodes a chromatin protein that shares polytene chromosome-binding sites with Polycomb. Genes Dev. 1992 Feb;6(2):223-32. PMID:1346609
- ↑ Kim CA, Sawaya MR, Cascio D, Kim W, Bowie JU. Structural organization of a Sex-comb-on-midleg/polyhomeotic copolymer. J Biol Chem. 2005 Jul 29;280(30):27769-75. Epub 2005 May 19. PMID:15905166 doi:10.1074/jbc.M503055200
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