5zba
From Proteopedia
(Difference between revisions)
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<StructureSection load='5zba' size='340' side='right' caption='[[5zba]], [[Resolution|resolution]] 3.50Å' scene=''> | <StructureSection load='5zba' size='340' side='right' caption='[[5zba]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5zba]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZBA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZBA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5zba]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspfu Aspfu] and [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=5ZBA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZBA FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5zb9|5zb9]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5zb9|5zb9]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AFUA_5G09540 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=330879 ASPFU]), asf1, AFUA_3G11030 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=330879 ASPFU]), HHT1, YBR010W, YBR0201, HHT2, SIN2, YNL031C, N2749 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), HHF1, YBR009C, YBR0122, HHF2, YNL030W, N2752 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=5zba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zba OCA], [http://pdbe.org/5zba PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zba RCSB], [http://www.ebi.ac.uk/pdbsum/5zba PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zba 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=5zba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zba OCA], [http://pdbe.org/5zba PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zba RCSB], [http://www.ebi.ac.uk/pdbsum/5zba PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zba ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/ASF1_ASPFU ASF1_ASPFU]] Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. | [[http://www.uniprot.org/uniprot/ASF1_ASPFU ASF1_ASPFU]] Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Rtt109 is a unique histone acetyltransferase acetylating histone H3 lysine 56 (H3K56), a modification critical for DNA replication-coupled nucleosome assembly and genome stability. In cells, histone chaperone Asf1 is essential for H3K56 acetylation, yet the mechanisms for H3K56 specificity and Asf1 requirement remain unknown. We have determined the crystal structure of the Rtt109-Asf1-H3-H4 complex and found that unwinding of histone H3 alphaN, where K56 is normally located, and stabilization of the very C-terminal beta strand of histone H4 by Asf1 are prerequisites for H3K56 acetylation. Unexpectedly, an interaction between Rtt109 and the central helix of histone H3 is also required. The observed multiprotein, multisite substrate recognition mechanism among histone modification enzymes provides mechanistic understandings of Rtt109 and Asf1 in H3K56 acetylation, as well as valuable insights into substrate recognition by histone modification enzymes in general. | ||
| + | |||
| + | Multisite Substrate Recognition in Asf1-Dependent Acetylation of Histone H3 K56 by Rtt109.,Zhang L, Serra-Cardona A, Zhou H, Wang M, Yang N, Zhang Z, Xu RM Cell. 2018 Aug 9;174(4):818-830.e11. doi: 10.1016/j.cell.2018.07.005. Epub 2018, Jul 26. PMID:30057113<ref>PMID:30057113</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5zba" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Aspfu]] | ||
| + | [[Category: Baker's yeast]] | ||
[[Category: Serra-Cardona, A]] | [[Category: Serra-Cardona, A]] | ||
[[Category: Wang, M]] | [[Category: Wang, M]] | ||
Revision as of 06:30, 22 August 2018
Crystal structure of Rtt109-Asf1-H3-H4-CoA complex
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