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==Crystal Structure of the S. pombe Peptidase Homology Domain of FACT complex subunit Spt16 (form B)==
==Crystal Structure of the S. pombe Peptidase Homology Domain of FACT complex subunit Spt16 (form B)==
<StructureSection load='3cb6' size='340' side='right' caption='[[3cb6]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
<StructureSection load='3cb6' size='340' side='right'caption='[[3cb6]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3cb6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_356 Cbs 356]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CB6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CB6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3cb6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CB6 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3biq|3biq]], [[3bip|3bip]], [[3bit|3bit]], [[3cb5|3cb5]]</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]] 1.84&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spt16 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4896 CBS 356])</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=3cb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cb6 OCA], [https://pdbe.org/3cb6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cb6 RCSB], [https://www.ebi.ac.uk/pdbsum/3cb6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cb6 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=3cb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cb6 OCA], [http://pdbe.org/3cb6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cb6 RCSB], [http://www.ebi.ac.uk/pdbsum/3cb6 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SPT16_SCHPO SPT16_SCHPO]] 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 (By similarity).  
[https://www.uniprot.org/uniprot/SPT16_SCHPO SPT16_SCHPO] 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 (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cb/3cb6_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cb/3cb6_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cbs 356]]
[[Category: Large Structures]]
[[Category: Bortfeld-Miller, M]]
[[Category: Schizosaccharomyces pombe]]
[[Category: Hothorn, M]]
[[Category: Bortfeld-Miller M]]
[[Category: Ladurner, A G]]
[[Category: Hothorn M]]
[[Category: Lejeune, E]]
[[Category: Ladurner AG]]
[[Category: Scheffzek, K]]
[[Category: Lejeune E]]
[[Category: Stuwe, T]]
[[Category: Scheffzek K]]
[[Category: Chromosomal protein]]
[[Category: Stuwe T]]
[[Category: Dna damage]]
[[Category: Dna repair]]
[[Category: Dna replication]]
[[Category: Histone binding module]]
[[Category: Histone h3/h4 chaperone]]
[[Category: Nucleus]]
[[Category: Peptidase homology domain]]
[[Category: Pita-bread fold]]
[[Category: Transcription]]
[[Category: Transcription regulation]]
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