3KO1

Cystal structure of thermosome from Acidianus tengchongensis strain S5

Summary for 3KO1

• Entry DOI: 10.2210/pdb3ko1/pdb
• Descriptor: Chaperonin, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• Functional Keywords: 9-fold symmetry, double ring, atp hydrolase, chaperone, nucleotide-binding
• Biological source: Acidianus tengchongensis
• Total number of polymer chains: 9
• Total formula weight: 541489.91

Authors

Huo, Y.,Zhang, K.,Hu, Z.,Wang, L.,Zhai, Y.,Zhou, Q.,Lander, G.,He, Y.,Zhu, J.,Xu, W.,Dong, Z.,Sun, F. (deposition date: 2009-11-12, release date: 2010-11-03, Last modification date: 2023-11-01)

Primary citation

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

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: 20947016
DOI: 10.1016/j.str.2010.07.009

Experimental method

X-RAY DIFFRACTION (3.7 Å)