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| | <StructureSection load='5wlf' size='340' side='right'caption='[[5wlf]], [[Resolution|resolution]] 1.40Å' scene=''> | | <StructureSection load='5wlf' size='340' side='right'caption='[[5wlf]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5wlf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WLF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WLF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5wlf]] is a 1 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=5WLF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WLF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5wle|5wle]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pps, CG6525, Dmel_CG6525 ([http://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=5wlf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wlf OCA], [https://pdbe.org/5wlf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wlf RCSB], [https://www.ebi.ac.uk/pdbsum/5wlf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wlf ProSAT]</span></td></tr> |
| - | <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=5wlf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wlf OCA], [http://pdbe.org/5wlf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wlf RCSB], [http://www.ebi.ac.uk/pdbsum/5wlf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wlf ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9VG78_DROME Q9VG78_DROME] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Klein, B J]] | + | [[Category: Klein BJ]] |
| - | [[Category: Kutateladze, T G]] | + | [[Category: Kutateladze TG]] |
| - | [[Category: Epigenetic]]
| + | |
| - | [[Category: Histone]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Phd]]
| + | |
| - | [[Category: Trimethylated]]
| + | |
| Structural highlights
Function
Q9VG78_DROME
Publication Abstract from PubMed
The protein partner of Sans-fille (PPS) and its human homolog DIDO mediate diverse chromatin activities, including the regulation of stemness genes in embryonic stem cells and splicing in Drosophila. Here, we show that the PHD fingers of PPS and DIDO recognize the histone mark H3K4me3 in a pH-dependent manner: the binding is enhanced at high pH values but is decreased at low pH. Structural analysis reveals that the pH dependency is due to the presence of a histidine residue in the K4me3-binding aromatic cage of PPS. The pH-dependent mechanism is conserved in DIDO but is lost in yeast Bye1. Acidification of cells leads to the accelerated efflux of endogenous DIDO, indicating the pH-dependent sensing of H3K4me3 in vivo. This novel mode for the recognition of H3K4me3 establishes the PHD fingers of PPS and DIDO as unique epigenetic readers and high pH sensors and suggests a role for the histidine switch during mitosis.
A Unique pH-Dependent Recognition of Methylated Histone H3K4 by PPS and DIDO.,Tencer AH, Gatchalian J, Klein BJ, Khan A, Zhang Y, Strahl BD, van Wely KHM, Kutateladze TG Structure. 2017 Sep 8. pii: S0969-2126(17)30262-9. doi:, 10.1016/j.str.2017.08.009. PMID:28919441[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tencer AH, Gatchalian J, Klein BJ, Khan A, Zhang Y, Strahl BD, van Wely KHM, Kutateladze TG. A Unique pH-Dependent Recognition of Methylated Histone H3K4 by PPS and DIDO. Structure. 2017 Sep 8. pii: S0969-2126(17)30262-9. doi:, 10.1016/j.str.2017.08.009. PMID:28919441 doi:http://dx.doi.org/10.1016/j.str.2017.08.009
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