Detection of a concerted conformational change in the ATPase domain of DnaK triggered by peptide binding.
Detection of a concerted conformational change in the ATPase domain of DnaK triggered by peptide binding.
复制标题
检测肽结合触发的 DnaK ATP 酶结构域中的协同构象变化。
DOI：
10.1016/s0014-5793(03)00207-2
复制
发表时间：
2003
期刊：
影响因子：
3.5
通讯作者：
Witt,StephanN
中科院分区：
文献类型：
--
作者：
Slepenkov,SergeyV;Witt,StephanN
The molecular chaperone DnaK is composed of two functional domains, the ATPase domain and the substrate-binding domain. In this report, we show that peptide binding to DnaK can be sensed in real time through a labeled nucleotide bound in the ATPase domain. Specifically, when N8-(4-N′-methylanthraniloylaminobutyl)-8-aminoadenosine 5′-triphosphate (MABA)–ATP·DnaK complexes are rapidly mixed with excess peptide, MABA fluorescence rapidly increases and the rate of increase is proportional to peptide concentration. Analysis of the formation traces yield on and off rate constants that are exactly equal to the rate constants obtained from experiments that directly probe peptide binding to DnaK. These results are the first to show that peptide binding to ATP·DnaK triggers a concerted conformational change in the ATPase domain.
