2h53

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(New page: 200px<br /><applet load="2h53" size="350" color="white" frame="true" align="right" spinBox="true" caption="2h53" /> '''Multiple distinct assemblies reveal conforma...)
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[[Image:2h53.gif|left|200px]]<br /><applet load="2h53" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2h53" />
 
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'''Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26'''<br />
 
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==Overview==
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==Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26==
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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.
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<SX load='2h53' size='340' side='right' viewer='molstar' caption='[[2h53]], [[Resolution|resolution]] 11.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2h53]] 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=2H53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H53 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 11.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h53 OCA], [https://pdbe.org/2h53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h53 RCSB], [https://www.ebi.ac.uk/pdbsum/2h53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h53 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HS16B_WHEAT HS16B_WHEAT]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h5/2h53_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2h53 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2H53 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H53 OCA].
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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__TOC__
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==Reference==
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</SX>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16843901 16843901]
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Buchner J]]
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[[Category: Buchner, J.]]
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[[Category: Chen S]]
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[[Category: Chen, S.]]
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[[Category: Franzmann TM]]
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[[Category: Franzmann, T.M.]]
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[[Category: Gowen B]]
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[[Category: Gowen, B.]]
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[[Category: Haslbeck M]]
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[[Category: Haslbeck, M.]]
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[[Category: Ignatiou A]]
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[[Category: Ignatiou, A.]]
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[[Category: Orlova EV]]
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[[Category: Orlova, E.V.]]
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[[Category: Saibil HR]]
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[[Category: Saibil, H.R.]]
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[[Category: Stromer T]]
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[[Category: Stromer, T.]]
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[[Category: Wang L]]
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[[Category: Wang, L.]]
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[[Category: White HE]]
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[[Category: White, H.E.]]
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[[Category: alpha-crystallin]]
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[[Category: chaperones]]
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[[Category: cryo-electron microscopy]]
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[[Category: heat shock proteins]]
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[[Category: single particle reconstruction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:14:35 2008''
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Current revision

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

2h53, resolution 11.50Å

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