6kmb

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<StructureSection load='6kmb' size='340' side='right'caption='[[6kmb]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='6kmb' size='340' side='right'caption='[[6kmb]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6kmb]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KMB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KMB FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6kmb]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KMB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KMB FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">STH1, NPS1, YIL126W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </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=6kmb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kmb OCA], [http://pdbe.org/6kmb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kmb RCSB], [http://www.ebi.ac.uk/pdbsum/6kmb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kmb 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=6kmb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kmb OCA], [http://pdbe.org/6kmb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kmb RCSB], [http://www.ebi.ac.uk/pdbsum/6kmb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kmb ProSAT]</span></td></tr>
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== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/STH1_YEAST STH1_YEAST]] Catalytic component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is the essential ATPase of the complex. It is a DNA translocase capable of nucleosome remodeling. Required for full expression of early meiotic genes. Essential for mitotic growth and repression of CHA1 expression. Also involved in G2 phase control.<ref>PMID:10025404</ref> <ref>PMID:10320476</ref> <ref>PMID:10329629</ref> <ref>PMID:12072455</ref> <ref>PMID:12183366</ref> <ref>PMID:12697820</ref> <ref>PMID:8980231</ref> <ref>PMID:9799253</ref>
[[http://www.uniprot.org/uniprot/STH1_YEAST STH1_YEAST]] Catalytic component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is the essential ATPase of the complex. It is a DNA translocase capable of nucleosome remodeling. Required for full expression of early meiotic genes. Essential for mitotic growth and repression of CHA1 expression. Also involved in G2 phase control.<ref>PMID:10025404</ref> <ref>PMID:10320476</ref> <ref>PMID:10329629</ref> <ref>PMID:12072455</ref> <ref>PMID:12183366</ref> <ref>PMID:12697820</ref> <ref>PMID:8980231</ref> <ref>PMID:9799253</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The Saccharomyces cerevisiae RSC (Remodel the Structure of Chromatin) complex is a chromatin-remodeling complex and plays essential roles in transcription regulation and DNA repair. The acetylation of H3 Lysine14 (H3K14Ac) enhances the RSC retention on nucleosomes and increases the remodeling activity of RSC. However, which RSC component recognizes H3K14Ac remains unclear. Here, we discovered that the bromodomain of the catalytic subunit Sth1 (Sth1BD) possessed the strongest affinity to H3K14Ac among all RSC bromodomains. The Sth1BD specifically recognized the K(Ac)PhiPhiR motif (Phi stands for any hydrophobic amino acid), including H3K14Ac and H4K20Ac. We determined the crystal structures of Sth1BD at 2.40 A resolution and Sth1BD-H3K14Ac complex at 1.40 A resolution. The extensive interfaces between Sth1BD and H36-21 facilitate the specific and robust binding of Sth1BD to H3K14Ac. Our studies provide insights into how the RSC complex recognizes H3K14Ac to orchestrate the crosstalk between histone acetylation and chromatin remodeling.
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The Structural Basis for Specific Recognition of H3K14 Acetylation by Sth1 in the RSC Chromatin Remodeling Complex.,Chen G, Li W, Yan F, Wang D, Chen Y Structure. 2019 Nov 6. pii: S0969-2126(19)30356-9. doi:, 10.1016/j.str.2019.10.015. PMID:31711754<ref>PMID:31711754</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6kmb" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Baker's yeast]]
[[Category: DNA helicase]]
[[Category: DNA helicase]]
[[Category: Large Structures]]
[[Category: Large Structures]]

Revision as of 08:44, 27 November 2019

Crystal structure of Sth1 bromodomain

PDB ID 6kmb

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