5umu

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'''Unreleased structure'''
 
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The entry 5umu is ON HOLD until Paper Publication
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==Crystal structure of the middle double PH domain of human FACT complex subunit SPT16==
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<StructureSection load='5umu' size='340' side='right' caption='[[5umu]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5umu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UMU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UMU FirstGlance]. <br>
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Description:
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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]], [[5umt|5umt]]</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=5umu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5umu OCA], [http://pdbe.org/5umu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5umu RCSB], [http://www.ebi.ac.uk/pdbsum/5umu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5umu ProSAT]</span></td></tr>
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</table>
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== 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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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Botuyan, M V]]
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[[Category: Heroux, A]]
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[[Category: Hu, Q]]
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[[Category: Mer, G]]
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[[Category: Su, D]]
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[[Category: Thompson, J R]]
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[[Category: Histone chaperone]]
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[[Category: Human fact]]
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[[Category: Ph domain]]
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[[Category: Transcription]]

Revision as of 05:51, 31 January 2018

Crystal structure of the middle double PH domain of human FACT complex subunit SPT16

5umu, resolution 1.90Å

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