1shs

<table><tr><td colspan='2'>[[1shs]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SHS FirstGlance]. <br>

</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=1shs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1shs OCA], [https://pdbe.org/1shs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1shs RCSB], [https://www.ebi.ac.uk/pdbsum/1shs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1shs ProSAT], [https://www.topsan.org/Proteins/BSGC/1shs TOPSAN]</span></td></tr>

[[https://www.uniprot.org/uniprot/HSPS_METJA HSPS_METJA]] Chaperone that confers thermal protection to other proteins.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The principal heat-shock proteins that have chaperone activity (that is, they protect newly made proteins from misfolding) belong to five conserved classes: HSP100, HSP90, HSP70, HSP60 and the small heat-shock proteins (sHSPs). The sHSPs can form large multimeric structures and have a wide range of cellular functions, including endowing cells with thermotolerance in vivo and being able to act as molecular chaperones in vitro; sHSPs do this by forming stable complexes with folding intermediates of their protein substrates. However, there is little information available about these structures or the mechanism by which substrates are protected from thermal denaturation by sHSPs. Here we report the crystal structure of a small heat-shock protein from Methanococcus jannaschii, a hyperthermophilic archaeon. The monomeric folding unit is a composite beta-sandwich in which one of the beta-strands comes from a neighbouring molecule. Twenty-four monomers form a hollow spherical complex of octahedral symmetry, with eight trigonal and six square 'windows'. The sphere has an outer diameter of 120 A and an inner diameter of 65 A.

Crystal structure of a small heat-shock protein.,Kim KK, Kim R, Kim SH Nature. 1998 Aug 6;394(6693):595-9. PMID:9707123<ref>PMID:9707123</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1shs" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 43067]]

[[Category: Structural genomic]]

[[Category: Kim, K K]]

[[Category: Kim, R]]

[[Category: Kim, S H]]

[[Category: PSI, Protein structure initiative]]