|
|
| Line 3: |
Line 3: |
| | <StructureSection load='2cu9' size='340' side='right'caption='[[2cu9]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='2cu9' size='340' side='right'caption='[[2cu9]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2cu9]] 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=2CU9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CU9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2cu9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cbs_356 Cbs 356]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CU9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PG0:2-(2-METHOXYETHOXY)ETHANOL'>PG0</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PG0:2-(2-METHOXYETHOXY)ETHANOL'>PG0</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2dze|2dze]], [[2z34|2z34]], [[2z3f|2z3f]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2dze|2dze]], [[2z34|2z34]], [[2z3f|2z3f]]</div></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=2cu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cu9 OCA], [http://pdbe.org/2cu9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cu9 RCSB], [http://www.ebi.ac.uk/pdbsum/2cu9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cu9 ProSAT], [http://www.topsan.org/Proteins/RSGI/2cu9 TOPSAN]</span></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=2cu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cu9 OCA], [https://pdbe.org/2cu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cu9 RCSB], [https://www.ebi.ac.uk/pdbsum/2cu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cu9 ProSAT], [https://www.topsan.org/Proteins/RSGI/2cu9 TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ASF1_SCHPO ASF1_SCHPO]] Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly.<ref>PMID:11856374</ref> | + | [[https://www.uniprot.org/uniprot/ASF1_SCHPO ASF1_SCHPO]] Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly.<ref>PMID:11856374</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 29: |
Line 29: |
| | </div> | | </div> |
| | <div class="pdbe-citations 2cu9" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 2cu9" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Anti-silencing factor 3D structures|Anti-silencing factor 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Structural highlights
Function
[ASF1_SCHPO] Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The assembly of core histones onto eukaryotic DNA is modulated by several histone chaperone complexes, including Asf1, CAF-1, and HIRA. Asf1 is a unique histone chaperone that participates in both the replication-dependent and replication-independent pathways. Here we report the crystal structures of the apo-form of fission yeast Asf1/Cia1 (SpAsf1N; residues 1-161) as well as its complexes with the B-domain of the fission yeast HIRA orthologue Hip1 (Hip1B) and the C-terminal region of the Cac2 subunit of CAF-1 (Cac2C). The mode of the fission yeast Asf1N-Hip1B recognition is similar to that of the human Asf1-HIRA recognition, suggesting that Asf1N recognition of Hip1B/HIRA is conserved from yeast to mammals. Interestingly, Hip1B and Cac2C show remarkably similar interaction modes with Asf1. The binding between Asf1N and Hip1B was almost completely abolished by the D37A and L60A/V62A mutations in Asf1N, indicating the critical role of salt bridge and van der Waals contacts in the complex formation. Consistently, both of the aforementioned Asf1 mutations also drastically reduced the binding to Cac2C. These results provide a structural basis for a mutually exclusive Asf1-binding model of CAF-1 and HIRA/Hip1, in which Asf1 and CAF-1 assemble histones H3/H4 (H3.1/H4 in vertebrates) in a replication-dependent pathway, whereas Asf1 and HIRA/Hip1 assemble histones H3/H4 (H3.3/H4 in vertebrates) in a replication-independent pathway.
Crystal structures of fission yeast histone chaperone Asf1 complexed with the Hip1 B-domain or the Cac2 C terminus.,Malay AD, Umehara T, Matsubara-Malay K, Padmanabhan B, Yokoyama S J Biol Chem. 2008 May 16;283(20):14022-31. Epub 2008 Mar 11. PMID:18334479[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Umehara T, Chimura T, Ichikawa N, Horikoshi M. Polyanionic stretch-deleted histone chaperone cia1/Asf1p is functional both in vivo and in vitro. Genes Cells. 2002 Jan;7(1):59-73. PMID:11856374
- ↑ Malay AD, Umehara T, Matsubara-Malay K, Padmanabhan B, Yokoyama S. Crystal structures of fission yeast histone chaperone Asf1 complexed with the Hip1 B-domain or the Cac2 C terminus. J Biol Chem. 2008 May 16;283(20):14022-31. Epub 2008 Mar 11. PMID:18334479 doi:10.1074/jbc.M800594200
|
