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-Structure paper
Title | Crystal structure of group II chaperonin in the open state. |
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Journal, issue, pages | Structure, Vol. 18, Issue 10, Page 1270-1279, Year 2010 |
Publish date | Oct 13, 2010 |
Authors | Yanwu Huo / Zhongjun Hu / Kai Zhang / Li Wang / Yujia Zhai / Qiangjun Zhou / Gabe Lander / Jiang Zhu / Yongzhi He / Xiaoyun Pang / Wei Xu / Mark Bartlam / Zhiyang Dong / Fei Sun / |
PubMed Abstract | 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 ...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 (rATcpnβ) in the open state from Acidianus tengchongensis. There is a ∼30° 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 rATcpnβ 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. |
External links | Structure / PubMed:20947016 / PubMed Central |
Methods | EM (single particle) / X-ray diffraction |
Resolution | 3.7 - 14.0 Å |
Structure data | EMDB-5154: EMDB-5157: EMDB-5159: PDB-3ko1: |
Chemicals | ChemComp-ADP: |
Source |
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Keywords | CHAPERONE / 9-fold symmetry / double ring / ATP hydrolase / Nucleotide-binding |