3c9c

From Proteopedia

(Difference between revisions)

Revision as of 13:52, 7 November 2018

Structural Basis of Histone H4 Recognition by p55

Structural highlights

3c9c is a 2 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	3c99
Gene:	Caf1 (DROME)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CAF1_DROME] Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; the nucleosome remodeling and deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; the nucleosome remodeling factor (NURF) complex, which catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin; and the polycomb group (PcG) repressor complex ESC-E(Z), which promotes repression of homeotic genes during development. Also required for transcriptional repression of E2F target genes by E2f2 and Rbf or Rbf2.^[1] ^[2] ^[3] ^[4] ^[5]

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

p55 is a common component of many chromatin-modifying complexes and has been shown to bind to histones. Here, we present a crystal structure of Drosophila p55 bound to a histone H4 peptide. p55, a predicted WD40 repeat protein, recognizes the first helix of histone H4 via a binding pocket located on the side of a beta-propeller structure. The pocket cannot accommodate the histone fold of H4, which must be altered to allow p55 binding. Reconstitution experiments show that the binding pocket is important to the function of p55-containing complexes. These data demonstrate that WD40 repeat proteins use various surfaces to direct the modification of histones.

Structural basis of histone H4 recognition by p55.,Song JJ, Garlick JD, Kingston RE Genes Dev. 2008 May 15;22(10):1313-8. Epub 2008 Apr 28. PMID:18443147^[6]

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

References

↑ Tyler JK, Bulger M, Kamakaka RT, Kobayashi R, Kadonaga JT. The p55 subunit of Drosophila chromatin assembly factor 1 is homologous to a histone deacetylase-associated protein. Mol Cell Biol. 1996 Nov;16(11):6149-59. PMID:8887645
↑ Martinez-Balbas MA, Tsukiyama T, Gdula D, Wu C. Drosophila NURF-55, a WD repeat protein involved in histone metabolism. Proc Natl Acad Sci U S A. 1998 Jan 6;95(1):132-7. PMID:9419341
↑ Gdula DA, Sandaltzopoulos R, Tsukiyama T, Ossipow V, Wu C. Inorganic pyrophosphatase is a component of the Drosophila nucleosome remodeling factor complex. Genes Dev. 1998 Oct 15;12(20):3206-16. PMID:9784495
↑ Beall EL, Manak JR, Zhou S, Bell M, Lipsick JS, Botchan MR. Role for a Drosophila Myb-containing protein complex in site-specific DNA replication. Nature. 2002 Dec 19-26;420(6917):833-7. PMID:12490953 doi:10.1038/nature01228
↑ Taylor-Harding B, Binne UK, Korenjak M, Brehm A, Dyson NJ. p55, the Drosophila ortholog of RbAp46/RbAp48, is required for the repression of dE2F2/RBF-regulated genes. Mol Cell Biol. 2004 Oct;24(20):9124-36. PMID:15456884 doi:10.1128/MCB.24.20.9124-9136.2004
↑ Song JJ, Garlick JD, Kingston RE. Structural basis of histone H4 recognition by p55. Genes Dev. 2008 May 15;22(10):1313-8. Epub 2008 Apr 28. PMID:18443147 doi:10.1101/gad.1653308

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3c9c"

@@ Line 1: / Line 1: @@
 ==Structural Basis of Histone H4 Recognition by p55==
 <StructureSection load='3c9c' size='340' side='right' caption='[[3c9c]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3c99|3c99]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Caf1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=3c9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c9c OCA], [http://pdbe.org/3c9c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c9c RCSB], [http://www.ebi.ac.uk/pdbsum/3c9c PDBsum]</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=3c9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c9c OCA], [http://pdbe.org/3c9c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c9c RCSB], [http://www.ebi.ac.uk/pdbsum/3c9c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3c9c ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/3c9c_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/3c9c_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

3c9c

From Proteopedia

Revision as of 13:52, 7 November 2018

Structural Basis of Histone H4 Recognition by p55

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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