Journal
STRUCTURE
Volume 18, Issue 10, Pages 1270-1279Publisher
CELL PRESS
DOI: 10.1016/j.str.2010.07.009
Keywords
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Funding
- NSFC [30770496, 30721003]
- 973 project [2006CB806506, 2006CB911001]
- Chinese Academy of Sciences [KGCX1-YW-13]
- 863 project [2007AA100604]
- K.C. Wong Education Foundation, Hong Kong
- National Institute of Health through the National Center for Research Resources [RR17573]
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Thermosomes are group II chaperonins responsible for protein refolding in an ATP-dependent manner. Little is known regarding the conformational changes of thermosomes during their functional cycle due to a lack of high-resolution structure in the open state. Here, we report the first complete crystal structure of thermosome (rATcpn beta) in the open state from Acidianus tengchongensis. There is a 300 rotation of the apical and lid domains compared with the previous closed structure. Besides, the structure reveals a conspicuous hydrophobic patch in the lid domain, and residues locating in this patch are conserved across species. Both the closed and open forms of rATcpn beta were also reconstructed by electron microscopy (EM). Structural fitting revealed the detailed conformational change from the open to the closed state. Structural comparison as well as protease K digestion indicated only ATP binding without hydrolysis does not induce chamber closure of thermosome.
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