2z34

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of SpCia1/Asf1 complex with Hip1

Structural highlights

2z34 is a 4 chain structure with sequence from Schizosaccharomyces pombe and Schizosaccharomyces pombe 972h-. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.4Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HIR1_SCHPO Probably required for replication-independent chromatin assembly. Required for transcriptional silencing in the outer repeat (otr) centromeric repeats and the Tf2 long terminal repeat retrotransposons. Repressor of histone gene transcription in G1 arrested cells. Required for repression of htb1 gene expression outside of S phase.^[1] ^[2]

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Blackwell C, Martin KA, Greenall A, Pidoux A, Allshire RC, Whitehall SK. The Schizosaccharomyces pombe HIRA-like protein Hip1 is required for the periodic expression of histone genes and contributes to the function of complex centromeres. Mol Cell Biol. 2004 May;24(10):4309-20. PMID:15121850
↑ Greenall A, Williams ES, Martin KA, Palmer JM, Gray J, Liu C, Whitehall SK. Hip3 interacts with the HIRA proteins Hip1 and Slm9 and is required for transcriptional silencing and accurate chromosome segregation. J Biol Chem. 2006 Mar 31;281(13):8732-9. Epub 2006 Jan 22. PMID:16428807 doi:http://dx.doi.org/M512170200
↑ 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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2z34"

@@ Line 1: / Line 1: @@
 ==Crystal structure of SpCia1/Asf1 complex with Hip1==
-<StructureSection load='2z34' size='340' side='right' caption='[[2z34]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+<StructureSection load='2z34' size='340' side='right'caption='[[2z34]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2z34]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z34 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Z34 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2z34]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe] and [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z34 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z34 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2cu9|2cu9]], [[2dze|2dze]]</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]] 2.4&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cia1, asf1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4896 Schizosaccharomyces pombe])</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=2z34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z34 OCA], [https://pdbe.org/2z34 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z34 RCSB], [https://www.ebi.ac.uk/pdbsum/2z34 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z34 ProSAT]</span></td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2z34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z34 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2z34 RCSB], [http://www.ebi.ac.uk/pdbsum/2z34 PDBsum]</span></td></tr>
+</table>
-<table>
+== Function ==
+[https://www.uniprot.org/uniprot/HIR1_SCHPO HIR1_SCHPO] Probably required for replication-independent chromatin assembly. Required for transcriptional silencing in the outer repeat (otr) centromeric repeats and the Tf2 long terminal repeat retrotransposons. Repressor of histone gene transcription in G1 arrested cells. Required for repression of htb1 gene expression outside of S phase.<ref>PMID:15121850</ref> <ref>PMID:16428807</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z3/2z34_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z3/2z34_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2z34 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 25: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2z34" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Anti-silencing factor|Anti-silencing factor]]
+*[[Anti-silencing factor 3D structures|Anti-silencing factor 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Schizosaccharomyces pombe]]
-[[Category: Malay, A D.]]
+[[Category: Schizosaccharomyces pombe 972h-]]
-[[Category: Padmanabhan, B.]]
+[[Category: Malay AD]]
-[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
+[[Category: Padmanabhan B]]
-[[Category: Yokoyama, S.]]
+[[Category: Yokoyama S]]
-[[Category: Chaperone]]
-[[Category: Chromatin regulation]]
-[[Category: Chromatin regulator]]
-[[Category: Histone chaperone]]
-[[Category: National project on protein structural and functional analyse]]
-[[Category: Nppsfa]]
-[[Category: Nucleosome disassmebly/assembly]]
-[[Category: Nucleus]]
-[[Category: Repressor]]
-[[Category: Riken structural genomics/proteomics initiative]]
-[[Category: Rsgi]]
-[[Category: Structural genomic]]
-[[Category: Transcription]]
-[[Category: Transcription regulation]]
-[[Category: Wd repeat]]

2z34

From Proteopedia

Current revision

Crystal structure of SpCia1/Asf1 complex with Hip1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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