3KO1
Cystal structure of thermosome from Acidianus tengchongensis strain S5
3KO1 の概要
| エントリーDOI | 10.2210/pdb3ko1/pdb |
| 分子名称 | Chaperonin, ADENOSINE-5'-DIPHOSPHATE (2 entities in total) |
| 機能のキーワード | 9-fold symmetry, double ring, atp hydrolase, chaperone, nucleotide-binding |
| 由来する生物種 | Acidianus tengchongensis |
| タンパク質・核酸の鎖数 | 9 |
| 化学式量合計 | 541489.91 |
| 構造登録者 | |
| 主引用文献 | Huo, Y.,Hu, Z.,Zhang, K.,Wang, L.,Zhai, Y.,Zhou, Q.,Lander, G.,Zhu, J.,He, Y.,Pang, X.,Xu, W.,Bartlam, M.,Dong, Z.,Sun, F. Crystal structure of group II chaperonin in the open state. Structure, 18:1270-1279, 2010 Cited by 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 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. PubMed: 20947016DOI: 10.1016/j.str.2010.07.009 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.7 Å) |
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