4pq0

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(New page: '''Unreleased structure''' The entry 4pq0 is ON HOLD Authors: Liu, H. Description: Crystal structure of POB3 middle domain at 1.65A)
Current revision (08:58, 20 March 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 4pq0 is ON HOLD
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==Crystal structure of POB3 middle domain at 1.65A==
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<StructureSection load='4pq0' size='340' side='right'caption='[[4pq0]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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Authors: Liu, H.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4pq0]] is a 1 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=4PQ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PQ0 FirstGlance]. <br>
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Description: Crystal structure of POB3 middle domain at 1.65A
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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]] 1.65&#8491;</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=MLA:MALONIC+ACID'>MLA</scene></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=4pq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pq0 OCA], [https://pdbe.org/4pq0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pq0 RCSB], [https://www.ebi.ac.uk/pdbsum/4pq0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pq0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/POB3_YEAST POB3_YEAST] 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. Transcription elongation is promoted by the repression of transcription initiation from cryptic sites. Also acts in establishing transcription initiation complexes and promotes SPT15/TBP-binding to a TATA box. Together with replication factor-A protein (RPA), FACT may play a role in nucleosome deposition during DNA replication.<ref>PMID:10413469</ref> <ref>PMID:10924459</ref> <ref>PMID:11432837</ref> <ref>PMID:12524332</ref> <ref>PMID:14585989</ref> <ref>PMID:12934008</ref> <ref>PMID:15082784</ref> <ref>PMID:15987999</ref> <ref>PMID:16678108</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: Large Structures]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Liu H]]

Current revision

Crystal structure of POB3 middle domain at 1.65A

PDB ID 4pq0

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