Crystal structure of a small heat-shock protein

Kyeong Kyu Kim, Rosalind Kim and Sung-Hou Kim ()
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Kyeong Kyu Kim: University of California at Berkeley
Rosalind Kim: University of California at Berkeley
Sung-Hou Kim: University of California at Berkeley

Nature, 1998, vol. 394, issue 6693, 595-599

Abstract: 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 β-sandwich in which one of the β-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.

Date: 1998
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DOI: 10.1038/29106

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