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==The crystal structure of a subunit of the heterodimeric FACT complex (Spt16p-Pob3p).==
==The crystal structure of a subunit of the heterodimeric FACT complex (Spt16p-Pob3p).==
<StructureSection load='3f5r' size='340' side='right' caption='[[3f5r]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='3f5r' size='340' side='right'caption='[[3f5r]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3f5r]] 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=3F5R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3F5R FirstGlance]. <br>
<table><tr><td colspan='2'>[[3f5r]] 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=3F5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F5R FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.7&#8491;</td></tr>
<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>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">POB3, Saccharomyces cerevisiae, YML069W ([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=3f5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f5r OCA], [https://pdbe.org/3f5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f5r RCSB], [https://www.ebi.ac.uk/pdbsum/3f5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f5r ProSAT], [https://www.topsan.org/Proteins/MCSG/3f5r TOPSAN]</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=3f5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f5r OCA], [http://pdbe.org/3f5r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3f5r RCSB], [http://www.ebi.ac.uk/pdbsum/3f5r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3f5r ProSAT], [http://www.topsan.org/Proteins/MCSG/3f5r TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>
[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>  
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Cui, H]]
[[Category: Edwards, A]]
[[Category: Joachimiak, A]]
[[Category: Structural genomic]]
[[Category: Savchenko, A]]
[[Category: Tan, K]]
[[Category: Xu, X]]
[[Category: Apc7736]]
[[Category: Chromosomal protein]]
[[Category: Dna damage]]
[[Category: Dna repair]]
[[Category: Dna replication]]
[[Category: Mcsg]]
[[Category: Nucleus]]
[[Category: Phosphoprotein]]
[[Category: PSI, Protein structure initiative]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Transcription]]
[[Category: Cui H]]
[[Category: Transcription regulation]]
[[Category: Edwards A]]
[[Category: Transcription regulator]]
[[Category: Joachimiak A]]
[[Category: Savchenko A]]
[[Category: Tan K]]
[[Category: Xu X]]

Latest revision as of 21:58, 29 November 2023

The crystal structure of a subunit of the heterodimeric FACT complex (Spt16p-Pob3p).The crystal structure of a subunit of the heterodimeric FACT complex (Spt16p-Pob3p).

Structural highlights

3f5r is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

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.[1] [2] [3] [4] [5] [6] [7] [8] [9]

References

  1. ↑ Wittmeyer J, Joss L, Formosa T. Spt16 and Pob3 of Saccharomyces cerevisiae form an essential, abundant heterodimer that is nuclear, chromatin-associated, and copurifies with DNA polymerase alpha. Biochemistry. 1999 Jul 13;38(28):8961-71. PMID:10413469 doi:http://dx.doi.org/10.1021/bi982851d
  2. ↑ Schlesinger MB, Formosa T. POB3 is required for both transcription and replication in the yeast Saccharomyces cerevisiae. Genetics. 2000 Aug;155(4):1593-606. PMID:10924459
  3. ↑ Formosa T, Eriksson P, Wittmeyer J, Ginn J, Yu Y, Stillman DJ. Spt16-Pob3 and the HMG protein Nhp6 combine to form the nucleosome-binding factor SPN. EMBO J. 2001 Jul 2;20(13):3506-17. PMID:11432837 doi:http://dx.doi.org/10.1093/emboj/20.13.3506
  4. ↑ Formosa T, Ruone S, Adams MD, Olsen AE, Eriksson P, Yu Y, Rhoades AR, Kaufman PD, Stillman DJ. Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause dependence on the Hir/Hpc pathway: polymerase passage may degrade chromatin structure. Genetics. 2002 Dec;162(4):1557-71. PMID:12524332
  5. ↑ Mason PB, Struhl K. The FACT complex travels with elongating RNA polymerase II and is important for the fidelity of transcriptional initiation in vivo. Mol Cell Biol. 2003 Nov;23(22):8323-33. PMID:14585989
  6. ↑ Kaplan CD, Laprade L, Winston F. Transcription elongation factors repress transcription initiation from cryptic sites. Science. 2003 Aug 22;301(5636):1096-9. PMID:12934008 doi:http://dx.doi.org/10.1126/science.1087374
  7. ↑ Rhoades AR, Ruone S, Formosa T. Structural features of nucleosomes reorganized by yeast FACT and its HMG box component, Nhp6. Mol Cell Biol. 2004 May;24(9):3907-17. PMID:15082784
  8. ↑ Biswas D, Yu Y, Prall M, Formosa T, Stillman DJ. The yeast FACT complex has a role in transcriptional initiation. Mol Cell Biol. 2005 Jul;25(14):5812-22. PMID:15987999 doi:http://dx.doi.org/25/14/5812
  9. ↑ VanDemark AP, Blanksma M, Ferris E, Heroux A, Hill CP, Formosa T. The structure of the yFACT Pob3-M domain, its interaction with the DNA replication factor RPA, and a potential role in nucleosome deposition. Mol Cell. 2006 May 5;22(3):363-74. PMID:16678108 doi:10.1016/j.molcel.2006.03.025

3f5r, resolution 1.70Å

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