4fip: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:4fip.jpg|left|200px]]
-{{STRUCTURE_4fip|  PDB=4fip  |  SCENE=  }}
+==Structure of the SAGA Ubp8(S144N)/Sgf11(1-72, Delta-ZnF)/Sus1/Sgf73 DUB module==
+<StructureSection load='4fip' size='340' side='right'caption='[[4fip]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4fip]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FIP FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.686&#8491;</td></tr>
+<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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fip OCA], [https://pdbe.org/4fip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fip RCSB], [https://www.ebi.ac.uk/pdbsum/4fip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fip ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/UBP8_YEAST UBP8_YEAST] Functions as histone deubiquitinating component of the transcription regulatory histone acetylation (HAT) complexes SAGA and SLIK. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. Together with SGF11, is required for histone H2B deubiquitination.<ref>PMID:10026213</ref> <ref>PMID:14660634</ref> <ref>PMID:15657441</ref>
-===Structure of the SAGA Ubp8(S144N)/Sgf11(1-72, Delta-ZnF)/Sus1/Sgf73 DUB module===
+==See Also==
+*[[SAGA-associated factor|SAGA-associated factor]]
-{{ABSTRACT_PUBMED_22771212}}
+*[[Thioesterase 3D structures|Thioesterase 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-[[4fip]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FIP OCA].
+__TOC__
+</StructureSection>
-==Reference==
+[[Category: Large Structures]]
-<ref group="xtra">PMID:022771212</ref><references group="xtra"/>
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Saccharomyces cerevisiae]]
+[[Category: Ringel AE]]
-[[Category: Ubiquitinyl hydrolase 1]]
+[[Category: Samara NL]]
-[[Category: Ringel, A E.]]
+[[Category: Wolberger C]]
-[[Category: Samara, N L.]]
-[[Category: Wolberger, C.]]
-[[Category: Deubiquitination]]
-[[Category: Domain-swapping]]
-[[Category: Hydrolase]]
-[[Category: Nucleosome]]
-[[Category: Transcription]]