1erj: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
 
(One intermediate revision by the same user not shown)
Line 3: Line 3:
<StructureSection load='1erj' size='340' side='right'caption='[[1erj]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='1erj' size='340' side='right'caption='[[1erj]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1erj]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ERJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ERJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[1erj]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ERJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ERJ FirstGlance]. <br>
</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=1erj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1erj OCA], [https://pdbe.org/1erj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1erj RCSB], [https://www.ebi.ac.uk/pdbsum/1erj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1erj ProSAT]</span></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]] 2.3&#8491;</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=1erj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1erj OCA], [https://pdbe.org/1erj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1erj RCSB], [https://www.ebi.ac.uk/pdbsum/1erj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1erj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/TUP1_YEAST TUP1_YEAST]] Acts as component of the CYC8-TUP1 corepressor complex which is involved in the repression of many genes in a wide variety of physiological processes including heme-regulated and catabolite repressed genes. May also be involved in the derepression of at least some target genes. The complex is recruited to target genes by interaction with DNA-bound transcriptional repressors, like MATALPHA2, MIG1, RFX1 and SKO1. The complex recruits histone deacetylases to produce a repressive chromatin structure, interacts with hypoacetylated N-terminal tails of histones H3 and H4 that have been programmed for repression by the action of histone deacetylases and interferes directly with the transcriptional machinery by associating with the RNA polymerase II mediator complex.<ref>PMID:2247069</ref> <ref>PMID:11069890</ref> <ref>PMID:10722672</ref> <ref>PMID:11230135</ref> <ref>PMID:11172717</ref> <ref>PMID:11784848</ref> <ref>PMID:14665463</ref>
[https://www.uniprot.org/uniprot/TUP1_YEAST TUP1_YEAST] Acts as component of the CYC8-TUP1 corepressor complex which is involved in the repression of many genes in a wide variety of physiological processes including heme-regulated and catabolite repressed genes. May also be involved in the derepression of at least some target genes. The complex is recruited to target genes by interaction with DNA-bound transcriptional repressors, like MATALPHA2, MIG1, RFX1 and SKO1. The complex recruits histone deacetylases to produce a repressive chromatin structure, interacts with hypoacetylated N-terminal tails of histones H3 and H4 that have been programmed for repression by the action of histone deacetylases and interferes directly with the transcriptional machinery by associating with the RNA polymerase II mediator complex.<ref>PMID:2247069</ref> <ref>PMID:11069890</ref> <ref>PMID:10722672</ref> <ref>PMID:11230135</ref> <ref>PMID:11172717</ref> <ref>PMID:11784848</ref> <ref>PMID:14665463</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 31: Line 32:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Johnson, A D]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Redd, M J]]
[[Category: Johnson AD]]
[[Category: Sprague, E R]]
[[Category: Redd MJ]]
[[Category: Wolberger, C]]
[[Category: Sprague ER]]
[[Category: Beta-propeller]]
[[Category: Wolberger C]]
[[Category: Transcription inhibitor]]
Retrieved from "https://proteopedia.org/1erj"