A Distinct Meta-active Conformation in the 1.1-Å Resolution Structure of Wild-type ApoCheY*
A Distinct Meta-active Conformation in the 1.1-Å Resolution Structure of Wild-type ApoCheY*
复制标题
野生型 ApoCheY* 1.1-Å 分辨率结构中独特的元活性构象
DOI:
--
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发表时间:
2001
影响因子:
4.8
通讯作者:
K. Volz
中科院分区:
文献类型:
--
作者:
M. Simonović;K. Volz
CheY is the best characterized member of the response regulator superfamily, and as such it has become the principal model for understanding the initial molecular mechanisms of signaling in two-component systems. Normal signaling by response regulators requires phosphorylation, in combination with an activation mechanism whose conformational effects are not completely understood. CheY activation involves three events, phosphorylation, a conformational change in the β4–α4loop, and a rotational restriction of the side chain of tyrosine 106. An outstanding question concerns the nature of an active conformation in the apoCheY population. The details of this 1.08-Å resolution crystal structure of wild-type apoCheY shows the β4–α4 loop in two distinctly different conformations that sterically correlate with the two rotameric positions of the tyrosine 106 side chain. One of these conformational states of CheY is the inactive form, and we propose that the other is a meta-active form, responsible for the active properties seen in apoCheY.
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DOI:
10.1016/s0021-9258(18)92982-0
发表时间:
1991-05
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
G. Lukat;B. Lee;J. Mottonen;Ann M Stock;J. Stock
通讯作者:
G. Lukat;B. Lee;J. Mottonen;Ann M Stock;J. Stock
DOI:
10.2210/pdb3chy/pdb
发表时间:
1993-01
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
K. Volz;Philip Matsumura
通讯作者:
K. Volz;Philip Matsumura
影响因子:
2.9
作者:
BARAK, R;EISENBACH, M
通讯作者:
EISENBACH, M
影响因子:
3.2
作者:
Schär, J;Sickmann, A;Beier, D
通讯作者:
Beier, D
影响因子:
56.9
作者:
Volkman, BF;Lipson, D;Kern, D
通讯作者:
Kern, D