|
|
| (4 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | + | |
| | ==Structure of the Vps75-Rtt109 histone chaperone-lysine acetyltransferase complex (Full-length proteins in space group P6122)== | | ==Structure of the Vps75-Rtt109 histone chaperone-lysine acetyltransferase complex (Full-length proteins in space group P6122)== |
| - | <StructureSection load='3q66' size='340' side='right' caption='[[3q66]], [[Resolution|resolution]] 2.71Å' scene=''> | + | <StructureSection load='3q66' size='340' side='right'caption='[[3q66]], [[Resolution|resolution]] 2.71Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3q66]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q66 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q66 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3q66]] is a 3 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=3Q66 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q66 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.705Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3q68|3q68]]</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=3q66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q66 OCA], [https://pdbe.org/3q66 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q66 RCSB], [https://www.ebi.ac.uk/pdbsum/3q66 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q66 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">N0890, VPS75, YNL246W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), KIM2, L1377, REM50, RTT109, YLL002W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </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=3q66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q66 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q66 RCSB], [http://www.ebi.ac.uk/pdbsum/3q66 PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/VPS75_YEAST VPS75_YEAST]] Histone chaperone which acts as a cofactor stimulating the histone H3 'Lys-56' acetylation by RTT109. May be involved in vacuolar proteins sorting.<ref>PMID:12134085</ref> <ref>PMID:17320445</ref> [[http://www.uniprot.org/uniprot/RT109_YEAST RT109_YEAST]] Required for acetylation of 'Lys-56' of histone H3 (H3K56ac) which occurs in S phase and disappears during G(2)/M phase of the cell cycle and is involved in transcription DNA repair process. H3K56 acetylation weakens of the interaction between the histone core and the surrounding DNA in the nucleosomal particle and drives chromatin disassembly. Involved in regulation of Ty1 transposition.<ref>PMID:11779788</ref> <ref>PMID:17046836</ref> <ref>PMID:17369253</ref> <ref>PMID:17690098</ref> <ref>PMID:17320445</ref> <ref>PMID:17272722</ref> <ref>PMID:17272723</ref> <ref>PMID:18577595</ref> <ref>PMID:18723682</ref> | + | [https://www.uniprot.org/uniprot/VPS75_YEAST VPS75_YEAST] Histone chaperone which acts as a cofactor stimulating the histone H3 'Lys-56' acetylation by RTT109. May be involved in vacuolar proteins sorting.<ref>PMID:12134085</ref> <ref>PMID:17320445</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 20: |
Line 18: |
| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3q66" style="background-color:#fffaf0;"></div> |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Histone acetyltransferase|Histone acetyltransferase]] | + | *[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]] |
| | + | *[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Histone acetyltransferase]] | + | [[Category: Large Structures]] |
| | [[Category: Saccharomyces cerevisiae]] | | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Mer, G]] | + | [[Category: Mer G]] |
| - | [[Category: Su, D]] | + | [[Category: Su D]] |
| - | [[Category: Thompson, J R]] | + | [[Category: Thompson JR]] |
| - | [[Category: Chaperone-transferase complex]]
| + | |
| - | [[Category: Histone chaperone]]
| + | |
| - | [[Category: Lysine acetyltransferase]]
| + | |
| Structural highlights
Function
VPS75_YEAST Histone chaperone which acts as a cofactor stimulating the histone H3 'Lys-56' acetylation by RTT109. May be involved in vacuolar proteins sorting.[1] [2]
Publication Abstract from PubMed
The histone chaperone Vps75 presents the remarkable property of stimulating the Rtt109-dependent acetylation of several histone H3 lysine residues within (H3-H4)2 tetramers. To investigate this activation mechanism, we determined X-ray structures of full-length Vps75 in complex with full-length Rtt109 in two crystal forms. Both structures show similar asymmetric assemblies of a Vps75 dimer bound to an Rtt109 monomer. In the Vps75-Rtt109 complexes, the catalytic site of Rtt109 is confined to an enclosed space that can accommodate the N-terminal tail of histone H3 in (H3-H4)2. Investigation of Vps75-Rtt109-(H3-H4)2 and Vps75-(H3-H4)2 complexes by NMR spectroscopy-probed hydrogen/deuterium exchange suggests that Vps75 guides histone H3 in the catalytic enclosure. These findings clarify the basis for the enhanced acetylation of histone H3 tail residues by Vps75-Rtt109.
Structure and histone binding properties of the Vps75-Rtt109 chaperone-lysine acetyltransferase complex.,Su D, Hu Q, Zhou H, Thompson JR, Xu RM, Zhang Z, Mer G J Biol Chem. 2011 Mar 22. PMID:21454705[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bonangelino CJ, Chavez EM, Bonifacino JS. Genomic screen for vacuolar protein sorting genes in Saccharomyces cerevisiae. Mol Biol Cell. 2002 Jul;13(7):2486-501. PMID:12134085 doi:http://dx.doi.org/10.1091/mbc.02-01-0005
- ↑ Tsubota T, Berndsen CE, Erkmann JA, Smith CL, Yang L, Freitas MA, Denu JM, Kaufman PD. Histone H3-K56 acetylation is catalyzed by histone chaperone-dependent complexes. Mol Cell. 2007 Mar 9;25(5):703-12. Epub 2007 Feb 22. PMID:17320445 doi:S1097-2765(07)00086-X
- ↑ Su D, Hu Q, Zhou H, Thompson JR, Xu RM, Zhang Z, Mer G. Structure and histone binding properties of the Vps75-Rtt109 chaperone-lysine acetyltransferase complex. J Biol Chem. 2011 Mar 22. PMID:21454705 doi:10.1074/jbc.C111.220715
|
