2ygv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "2ygv" [edit=sysop:move=sysop])
Current revision (10:52, 20 December 2023) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 2ygv is ON HOLD
+
==Conserved N-terminal domain of the yeast Histone Chaperone Asf1 in complex with the C-terminal fragment of Rad53==
 +
<StructureSection load='2ygv' size='340' side='right'caption='[[2ygv]], [[Resolution|resolution]] 2.94&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2ygv]] is a 8 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=2YGV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YGV FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.94&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2ygv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ygv OCA], [https://pdbe.org/2ygv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ygv RCSB], [https://www.ebi.ac.uk/pdbsum/2ygv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ygv ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ASF1_YEAST ASF1_YEAST] Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Facilitates histone deposition through both replication-dependent and replication-independent chromatin assembly pathways. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with the HIR complex to promote replication-independent chromatin assembly, which may occur during transcription and DNA repair. May be required for the maintenance of a subset of replication elongation factors, including DNA polymerase epsilon, the RFC complex and PCNA, at stalled replication forks. Also required for acetylation of histone H3 on 'Lys-9' and 'Lys-56'.<ref>PMID:9290207</ref> <ref>PMID:10591219</ref> <ref>PMID:11412995</ref> <ref>PMID:11331602</ref> <ref>PMID:11731479</ref> <ref>PMID:11731480</ref> <ref>PMID:11404324</ref> <ref>PMID:11172707</ref> <ref>PMID:11856374</ref> <ref>PMID:11756556</ref> <ref>PMID:12093919</ref> <ref>PMID:14585955</ref> <ref>PMID:15071494</ref> <ref>PMID:15452122</ref> <ref>PMID:15175160</ref> <ref>PMID:15542829</ref> <ref>PMID:15542840</ref> <ref>PMID:15766286</ref> <ref>PMID:16303565</ref> <ref>PMID:15821127</ref> <ref>PMID:15901673</ref> <ref>PMID:16020781</ref> <ref>PMID:16143623</ref> <ref>PMID:16039596</ref> <ref>PMID:15632066</ref> <ref>PMID:15891116</ref> <ref>PMID:16141196</ref> <ref>PMID:15840725</ref> <ref>PMID:16815704</ref> <ref>PMID:16936140</ref> <ref>PMID:16582440</ref> <ref>PMID:16407267</ref> <ref>PMID:17046836</ref> <ref>PMID:16678113</ref> <ref>PMID:16501045</ref> <ref>PMID:16627621</ref> <ref>PMID:17107956</ref> <ref>PMID:17320445</ref> <ref>PMID:14680630</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The histone chaperone Asf1 and the checkpoint kinase Rad53 are found in a complex in budding yeast cells in the absence of genotoxic stress. Our data suggest that this complex involves at least three interaction sites. One site involves the H3-binding surface of Asf11 with an as yet undefined surface of Rad53. A second site is formed by the Rad53-FHA1 domain binding to Asf1-T(270) phosphorylated by casein kinase II. The third site involves the C-terminal 21 amino acids of Rad53 bound to the conserved Asf1 N-terminal domain. The structure of this site showed that the Rad53 C-terminus binds Asf1 in a remarkably similar manner to peptides derived from the histone cochaperones HirA and CAF-I. We call this binding motif, (R/K)R(I/A/V) (L/P), the AIP box for Asf1-Interacting Protein box. Furthermore, C-terminal Rad53-F(820) binds the same pocket of Asf1 as does histone H4-F(100). Thus Rad53 competes with histones H3-H4 and cochaperones HirA/CAF-I for binding to Asf1. Rad53 is phosphorylated and activated upon genotoxic stress. The Asf1-Rad53 complex dissociated when cells were treated with hydroxyurea but not methyl-methane-sulfonate, suggesting a regulation of the complex as a function of the stress. We identified a rad53 mutation that destabilized the Asf1-Rad53 complex and increased the viability of rad9 and rad24 mutants in conditions of genotoxic stress, suggesting that complex stability impacts the DNA damage response.
-
Authors: Jiao, Y., Seeger, K., Murciano, B., Ledu, M.H., Charbonnier, J.B., Legrand, P., Lautrette, A., Gaubert, A., Mousson, F., Guerois, R., Mann, C., Ochsenbein, F.
+
Surprising complexity of the Asf1 histone chaperone-Rad53 kinase interaction.,Jiao Y, Seeger K, Lautrette A, Gaubert A, Mousson F, Guerois R, Mann C, Ochsenbein F Proc Natl Acad Sci U S A. 2012 Feb 21;109(8):2866-71. Epub 2012 Feb 9. PMID:22323608<ref>PMID:22323608</ref>
-
Description: Conserved N-terminal domain of the yeast Histone Chaperone Asf1 in complex with the C-terminal fragment of Rad53
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2ygv" style="background-color:#fffaf0;"></div>
 +
 
 +
==See Also==
 +
*[[Anti-silencing factor 3D structures|Anti-silencing factor 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Saccharomyces cerevisiae]]
 +
[[Category: Charbonnier JB]]
 +
[[Category: Gaubert A]]
 +
[[Category: Guerois R]]
 +
[[Category: Jiao Y]]
 +
[[Category: Lautrette A]]
 +
[[Category: Ledu MH]]
 +
[[Category: Legrand P]]
 +
[[Category: Mann C]]
 +
[[Category: Mousson F]]
 +
[[Category: Murciano B]]
 +
[[Category: Ochsenbein F]]
 +
[[Category: Seeger K]]

Current revision

Conserved N-terminal domain of the yeast Histone Chaperone Asf1 in complex with the C-terminal fragment of Rad53

PDB ID 2ygv

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ygv"
Personal tools