Single-molecule analysis of nucleotide-dependent substrate binding by the protein unfoldase ClpA
Single-molecule analysis of nucleotide-dependent substrate binding by the protein unfoldase ClpA
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DOI：
10.1021/ja074168x
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发表时间：
2007-10-17
影响因子：
15
通讯作者：
Licht, Stuart
中科院分区：
文献类型：
--
作者：
Farbman, Mary E.;Gershenson, Anne;Licht, Stuart
对ClpAP蛋白酶的ClpA ATP酶组分的单分子荧光实验表明，ClpA以离散的高亲和力和低亲和力构象结合其肽底物。这些构象对应于ATP水解催化循环中的不同状态。在这些观察的基础上，我们提出，通过中央孔的ClpA的基板易位是由高和低亲和力状态之间的切换驱动。
Single-molecule fluorescence experiments on the ClpA ATPase component of the ClpAP protease demonstrate that ClpA binds its peptide substrates in discrete high- and low-affinity conformations. These conformations correspond to different states in the catalytic cycle of ATP hydrolysis. On the basis of these observations, we propose that translocation of substrates through the central pore of ClpA is driven by a switch between high- and low-affinity states.