Single-molecule analysis of nucleotide-dependent substrate binding by the protein unfoldase ClpA

被引：11
作者：
Farbman, Mary E.
Gershenson, Anne
Licht, Stuart
机构：
[1] MIT, Dept Chem, Cambridge, MA 02139 USA
[2] Brandeis Univ, Dept Chem, Waltham, MA 02454 USA
来源：
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2007年 / 129卷 / 41期
关键词：
D O I：
10.1021/ja074168x
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
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.
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页码：12378 / +
页数：3
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