Crystal structure of group II chaperonin in the open state.
Crystal structure of group II chaperonin in the open state.
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DOI：
10.1016/j.str.2010.07.009
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发表时间：
2010-10-13
期刊：
影响因子：
--
通讯作者：
Sun F
中科院分区：
文献类型：
--
作者：
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
热小体是负责蛋白质以ATP依赖性方式重折叠的II组伴侣蛋白。由于缺乏高分辨率的开放状态下的结构，对热小体在其功能周期中的构象变化知之甚少。本文报道了腾冲酸杆菌热小体（rATcpnβ）开放状态下的第一个完整晶体结构。与之前的封闭结构相比，顶端和盖域旋转约30°。此外，该结构揭示了一个明显的疏水补丁在盖域和残基定位在这个补丁是保守的物种。电镜下可观察到rATcpnβ的开放型和封闭型。结构拟合揭示了从开放状态到封闭状态的详细构象变化。结构比较以及蛋白酶K消化表明，只有ATP结合而不水解不会诱导热小体室关闭。
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 lack of high-resolution structure in open state. Here we report the first complete crystal structure of thermosome (rATcpnβ) in open state from Acidianus tengchongensis. There is a ~30° rotation of the apical and lid domains compared to 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 open to 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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DOI：
10.1107/s0907444904019158
发表时间：
2004-12-01
影响因子：
2.2
作者：
Emsley, P;Cowtan, K
通讯作者：
Cowtan, K
影响因子：
11.4
作者：
FRYDMAN, J;NIMMESGERN, E;HARTL, FU
通讯作者：
HARTL, FU
影响因子：
3
作者：
Crowther, RA;Henderson, R;Smith, JM
通讯作者：
Smith, JM
影响因子：
4.8
作者：
Iizuka, R;Yoshida, T;Yohda, M
通讯作者：
Yohda, M
DOI：
10.1107/s0907444998003254
发表时间：
1998-09-01
期刊：
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子：
--
作者：
Brunger, AT;Adams, PD;Warren, GL
通讯作者：
Warren, GL