View source for 4fei


==Hsp17.7 from Deinococcus radiodurans==
<StructureSection load='4fei' size='340' side='right'caption='[[4fei]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4fei]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans_R1 Deinococcus radiodurans R1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FEI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FEI 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]] 2.4&#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=4fei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fei OCA], [https://pdbe.org/4fei PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fei RCSB], [https://www.ebi.ac.uk/pdbsum/4fei PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fei ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9RTR5_DEIRA Q9RTR5_DEIRA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Small heat shock proteins (sHsps) are molecular chaperones that prevent the aggregation of nonnative proteins. The sHsps investigated to date mostly form large, oligomeric complexes. The typical bacterial scenario seemed to be a two-component sHsps system of two homologous sHsps, such as the Escherichia coli sHsps IbpA and IbpB. With a view to expand our knowledge on bacterial sHsps, we analyzed the sHsp system of the bacterium Deinococcus radiodurans, which is resistant against various stress conditions. D. radiodurans encodes two sHsps, termed Hsp17.7 and Hsp20.2. Surprisingly, Hsp17.7 forms only chaperone active dimers, although its crystal structure reveals the typical alpha-crystallin fold. In contrast, Hsp20.2 is predominantly a 36mer that dissociates into smaller oligomeric assemblies that bind substrate proteins stably. Whereas Hsp20.2 cooperates with the ATP-dependent bacterial chaperones in their refolding, Hsp17.7 keeps substrates in a refolding-competent state by transient interactions. In summary, we show that these two sHsps are strikingly different in their quaternary structures and chaperone properties, defining a second type of bacterial two-component sHsp system.

Alternative bacterial two-component small heat shock protein systems.,Bepperling A, Alte F, Kriehuber T, Braun N, Weinkauf S, Groll M, Haslbeck M, Buchner J Proc Natl Acad Sci U S A. 2012 Dec 11;109(50):20407-12. doi:, 10.1073/pnas.1209565109. Epub 2012 Nov 26. PMID:23184973<ref>PMID:23184973</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4fei" style="background-color:#fffaf0;"></div>

==See Also==
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Deinococcus radiodurans R1]]
[[Category: Large Structures]]
[[Category: Alte F]]
[[Category: Bepperling A]]
[[Category: Braun N]]
[[Category: Buchner J]]
[[Category: Groll M]]
[[Category: Haslbeck M]]
[[Category: Kriehuber T]]
[[Category: Weinkauf S]]