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| | ==Structure of the Spt16 Middle Domain Reveals Functional Features of the Histone Chaperone FACT== | | ==Structure of the Spt16 Middle Domain Reveals Functional Features of the Histone Chaperone FACT== |
| - | <StructureSection load='4ioy' size='340' side='right' caption='[[4ioy]], [[Resolution|resolution]] 1.94Å' scene=''> | + | <StructureSection load='4ioy' size='340' side='right'caption='[[4ioy]], [[Resolution|resolution]] 1.94Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ioy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IOY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IOY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ioy]] is a 1 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=4IOY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IOY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.945Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gcl|2gcl]], [[3gyp|3gyp]], [[3fss|3fss]], [[3to1|3to1]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPT16, CDC68, SSF1, YGL207W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=4ioy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ioy OCA], [https://pdbe.org/4ioy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ioy RCSB], [https://www.ebi.ac.uk/pdbsum/4ioy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ioy 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=4ioy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ioy OCA], [http://pdbe.org/4ioy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ioy RCSB], [http://www.ebi.ac.uk/pdbsum/4ioy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ioy ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/SPT16_YEAST SPT16_YEAST] |
| - | The histone chaperone FACT is an essential and abundant heterodimer found in all eukaryotes. Here we report a crystal structure of the middle domain of the large subunit of FACT (Spt16-M), revealing a double pleckstrin homology architecture. This motif was found previously in the Pob3-M domain of the small subunit of FACT, as well as in the related histone chaperone Rtt106, although Spt16-M is distinguished from these structures by the presence of an extended alpha-helix and a C-terminal addition. Consistent with our finding that the double pleckstrin homology structure is common to these three histone chaperone proteins and reports that Pob3 and Rtt106 double PH domains bind histones H3-H4, we also find that Spt16-M binds H3-H4 with low micromolar affinity. Our structure provides a framework for interpreting a large body of genetic data regarding the physiological functions of FACT, including the identification of potential interaction surfaces for binding histones or other proteins. We also describe a set of intragenic suppressors of a mutation of SPT16 that reveal important structural features of Spt16-M.
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| - | Structure of the Spt16 Middle Domain Reveals Functional Features of the Histone Chaperone FACT.,Kemble DJ, Whitby FG, Robinson H, McCullough LL, Formosa T, Hill CP J Biol Chem. 2013 Feb 15. PMID:23417676<ref>PMID:23417676</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 4ioy" style="background-color:#fffaf0;"></div>
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| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | + | [[Category: Large Structures]] |
| - | [[Category: Hill, C P]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Kemble, D J]] | + | [[Category: Hill CP]] |
| - | [[Category: Double pleckstrin homology domain]] | + | [[Category: Kemble DJ]] |
| - | [[Category: Fact]]
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| - | [[Category: H3-h4 histone]]
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| - | [[Category: Spt16]]
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| - | [[Category: Transcription]]
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