PMID:16810315
| Citation |
Thibault, G, Tsitrin, Y, Davidson, T, Gribun, A and Houry, WA (2006) Large nucleotide-dependent movement of the N-terminal domain of the ClpX chaperone. EMBO J. 25:3367-76 |
|---|---|
| Abstract |
The ClpXP ATPase-protease complex is a major component of the protein quality control machinery in the cell. A ClpX subunit consists of an N-terminal zinc binding domain (ZBD) and a C-terminal AAA+ domain. ClpX oligomerizes into a hexamer with the AAA+ domains forming the base of the hexamer and the ZBDs extending out of the base. Here, we report that ClpX switches between a capture and a feeding conformation. ZBDs in ClpX undergo large nucleotide-dependent block movement towards ClpP and into the AAA+ ring. This motion is modulated by the ClpX cofactor, SspB. Evidence for this movement was initially obtained by the surprising observation that an N-terminal extension on ClpX is clipped by bound ClpP in functional ClpXP complexes. Protease-protection, crosslinking, and light scattering experiments further support these findings. |
| Links |
PubMed PMC1523177 Online version:10.1038/sj.emboj.7601223 |
| Keywords |
Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/metabolism; Adenosine Triphosphatases/physiology; Bacterial Proteins/metabolism; Biological Transport, Active/physiology; Endopeptidase Clp/chemistry; Endopeptidase Clp/metabolism; Endopeptidase Clp/physiology; Escherichia coli/enzymology; Escherichia coli/physiology; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Escherichia coli Proteins/physiology; Molecular Chaperones/chemistry; Molecular Chaperones/metabolism; Molecular Chaperones/physiology; Nucleotides/physiology; Peptide Fragments/chemistry; Peptide Fragments/physiology; Protein Structure, Tertiary; Serine Endopeptidases/metabolism |
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