5umt

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==Crystal structure of N-terminal domain of human FACT complex subunit SPT16==
==Crystal structure of N-terminal domain of human FACT complex subunit SPT16==
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<StructureSection load='5umt' size='340' side='right' caption='[[5umt]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
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<StructureSection load='5umt' size='340' side='right'caption='[[5umt]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5umt]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UMT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UMT FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5umt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UMT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UMT FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.092&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5umr|5umr]], [[5ums|5ums]], [[5umu|5umu]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<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=5umt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5umt OCA], [http://pdbe.org/5umt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5umt RCSB], [http://www.ebi.ac.uk/pdbsum/5umt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5umt ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5umt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5umt OCA], [https://pdbe.org/5umt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5umt RCSB], [https://www.ebi.ac.uk/pdbsum/5umt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5umt ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SP16H_HUMAN SP16H_HUMAN]] Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II).<ref>PMID:10912001</ref> <ref>PMID:11239457</ref> <ref>PMID:12934006</ref> <ref>PMID:16713563</ref> <ref>PMID:9489704</ref> <ref>PMID:9836642</ref>
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[https://www.uniprot.org/uniprot/SP16H_HUMAN SP16H_HUMAN] Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II).<ref>PMID:10912001</ref> <ref>PMID:11239457</ref> <ref>PMID:12934006</ref> <ref>PMID:16713563</ref> <ref>PMID:9489704</ref> <ref>PMID:9836642</ref>
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==See Also==
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*[[Elongation factor 3D structures|Elongation factor 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Botuyan, M V]]
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[[Category: Homo sapiens]]
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[[Category: Hu, Q]]
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[[Category: Large Structures]]
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[[Category: Mer, G]]
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[[Category: Botuyan MV]]
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[[Category: Su, D]]
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[[Category: Hu Q]]
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[[Category: Thompson, J R]]
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[[Category: Mer G]]
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[[Category: Fact complex]]
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[[Category: Su D]]
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[[Category: Histone chaperone]]
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[[Category: Thompson JR]]
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[[Category: Spt16]]
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[[Category: Transcription]]
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Current revision

Crystal structure of N-terminal domain of human FACT complex subunit SPT16

PDB ID 5umt

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