5agc: Difference between revisions
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The | ==Crystallographic forms of the Vps75 tetramer== | ||
<StructureSection load='5agc' size='340' side='right' caption='[[5agc]], [[Resolution|resolution]] 4.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5agc]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AGC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AGC FirstGlance]. <br> | |||
</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=5agc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5agc OCA], [http://pdbe.org/5agc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5agc RCSB], [http://www.ebi.ac.uk/pdbsum/5agc PDBsum]</span></td></tr> | |||
</table> | |||
== 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> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
NAP-1 fold histone chaperones play an important role in escorting histones to and from sites of nucleosome assembly and disassembly. The two NAP-1 fold histone chaperones in budding yeast, Vps75 and Nap1, have previously been crystalized in a characteristic homodimeric conformation. In this study, a combination of small angle X-ray scattering, multi angle light scattering and pulsed electron-electron double resonance approaches were used to show that both Vps75 and Nap1 adopt ring-shaped tetrameric conformations in solution. This suggests that the formation of homotetramers is a common feature of NAP-1 fold histone chaperones. The tetramerisation of NAP-1 fold histone chaperones may act to shield acidic surfaces in the absence of histone cargo thus providing a 'self-chaperoning' type mechanism. | |||
The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution.,Bowman A, Hammond CM, Stirling A, Ward R, Shang W, El-Mkami H, Robinson DA, Svergun DI, Norman DG, Owen-Hughes T Nucleic Acids Res. 2014 May;42(9):6038-51. doi: 10.1093/nar/gku232. Epub 2014 Mar, 31. PMID:24688059<ref>PMID:24688059</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5agc" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hammond, C M]] | |||
[[Category: Owen-Hughes, T]] | [[Category: Owen-Hughes, T]] | ||
[[Category: Sundaramoorthy, R]] | [[Category: Sundaramoorthy, R]] | ||
[[Category: | [[Category: Chromatin]] | ||
[[Category: Histone chaperone]] | |||
[[Category: Nap1]] | |||
[[Category: Transport protein]] | |||
[[Category: Vacuolar protein sorting 75]] | |||
[[Category: Vps75]] | |||
Revision as of 15:02, 2 March 2016
Crystallographic forms of the Vps75 tetramer
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