2h50: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2h50]] is a 24 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=2H50 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H50 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2h50]] is a 24 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=2H50 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H50 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1gme|1gme]], [[2h53|2h53]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 10.8&#8491;</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=2h50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h50 OCA], [https://pdbe.org/2h50 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h50 RCSB], [https://www.ebi.ac.uk/pdbsum/2h50 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h50 ProSAT]</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=2h50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h50 OCA], [https://pdbe.org/2h50 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h50 RCSB], [https://www.ebi.ac.uk/pdbsum/2h50 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h50 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HS16B_WHEAT HS16B_WHEAT]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=2h50 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=2h50 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Small heat shock proteins are a superfamily of molecular chaperones that suppress protein aggregation and provide protection from cell stress. A key issue for understanding their action is to define the interactions of subunit domains in these oligomeric assemblies. Cryo-electron microscopy of yeast Hsp26 reveals two distinct forms, each comprising 24 subunits arranged in a porous shell with tetrahedral symmetry. The subunits form elongated, asymmetric dimers that assemble via trimeric contacts. Modifications of both termini cause rearrangements that yield a further four assemblies. Each subunit contains an N-terminal region, a globular middle domain, the alpha-crystallin domain, and a C-terminal tail. Twelve of the C termini form 3-fold assembly contacts which are inserted into the interior of the shell, while the other 12 C termini form contacts on the surface. Hinge points between the domains allow a variety of assembly contacts, providing the flexibility required for formation of supercomplexes with non-native proteins.
Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26.,White HE, Orlova EV, Chen S, Wang L, Ignatiou A, Gowen B, Stromer T, Franzmann TM, Haslbeck M, Buchner J, Saibil HR Structure. 2006 Jul;14(7):1197-204. PMID:16843901<ref>PMID:16843901</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2h50" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
<references/>
__TOC__
__TOC__
</SX>
</SX>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Buchner, J]]
[[Category: Buchner J]]
[[Category: Chen, S]]
[[Category: Chen S]]
[[Category: Franzmann, T M]]
[[Category: Franzmann TM]]
[[Category: Gowen, B]]
[[Category: Gowen B]]
[[Category: Haslbeck, M]]
[[Category: Haslbeck M]]
[[Category: Ignatiou, A]]
[[Category: Ignatiou A]]
[[Category: Orlova, E V]]
[[Category: Orlova EV]]
[[Category: Saibil, H R]]
[[Category: Saibil HR]]
[[Category: Stromer, T]]
[[Category: Stromer T]]
[[Category: Wang, L]]
[[Category: Wang L]]
[[Category: White, H E]]
[[Category: White HE]]
[[Category: Alpha-crystallin]]
[[Category: Chaperone]]
[[Category: Heat shock protein]]
[[Category: Single particle reconstruction]]

Latest revision as of 09:31, 14 February 2024

Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26

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