期刊论文详细信息
FEBS Letters
Towards a mechanism of AMP‐substrate inhibition in adenylate kinase from Escherichia coli
Haas, Elisha1  Sineva, Elena V.1  Sinev, Michael A.1  Ittah, Varda1 
[1] Department of Life Sciences, Bar-Ilan University, Ramat Gan 52900, Israel
关键词: Adenylate kinase;    Site-directed mutagenesis;    Time-resolved fluorescence;    Energy transfer;    Probe;    Substrate inhibition;   
DOI  :  10.1016/S0014-5793(96)01195-7
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

Crystallographic studies on adenylate kinase (AK) suggest that binding of ATP causes the LID domain of the enzyme to close over the ATP molecule (Schlauderer et al. (1996) J. Mol. Biol. 256, 223–227). The method of time-resolved fluorescence resonance energy transfer was applied to study the proposed structural change in AK from Escherichia coli. Two active derivatives of the (C77S, A73C, V142C)-AK mutant containing the excitation energy donor attached to one of the two cysteine residues and the acceptor attached to the other cysteine were prepared to monitor displacements of the LID domain in response to substrate binding. Binding of either ATP or AMP was accompanied by a ∼ 9 A decrease in the interprobe distances suggesting LID domain closure. Closure of the LID domain in response to AMP binding may be a possible reason for the strong AMP-substrate inhibition known for E. coli AK.

【 授权许可】

Unknown   

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