Crystal structure of a small heat-shock protein

Title
Crystal structure of a small heat-shock protein
Authors
김경규Rosalind Kim김성호
Keywords
crystal structure; small heat-shock protein
Issue Date
1998-08
Publisher
Nature
Citation
VOL 394, 595-599
Abstract
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 vivo1,2 and being able to act as molecular chaperones in vitro3, 4, 5, 6, 7, 8; sHSPs do this by forming stable complexes with folding intermediates of their protein substrates9,10. 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 -sandwich in which one of the -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 Å and an inner diameter of 65 Å.
URI
http://pubs.kist.re.kr/handle/201004/18695
ISSN
0028-0836
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