PMID:11163224
| Citation |
Ortega, J, Singh, SK, Ishikawa, T, Maurizi, MR and Steven, AC (2000) Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP. Mol. Cell 6:1515-21 |
|---|---|
| Abstract |
Binding and internalization of a protein substrate by E. coli ClpXP was investigated by electron microscopy. In sideviews of ATP gamma S-stabilized ClpXP complexes, a narrow axial channel was visible in ClpX, surrounded by protrusions on its distal surface. When substrate lambda O protein was added, extra density attached to this surface. Upon addition of ATP, this density disappeared as lambda O was degraded. When ATP was added to proteolytically inactive ClpXP-lambda O complexes, the extra density transferred to the center of ClpP and remained inside ClpP after separation from ClpX. We propose that substrates of ATP-dependent proteases bind to specific sites on the distal surface of the ATPase, and are subsequently unfolded and translocated into the internal chamber of the protease. |
| Links | |
| Keywords |
Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/metabolism; Adenosine Triphosphatases/ultrastructure; Adenosine Triphosphate/analogs & derivatives; Adenosine Triphosphate/metabolism; Bacteriophage lambda; Binding Sites; Dimerization; Endopeptidase Clp; Escherichia coli/enzymology; Escherichia coli Proteins; Image Processing, Computer-Assisted; Macromolecular Substances; Microscopy, Electron; Models, Molecular; Molecular Chaperones; Polylysine/metabolism; Protein Binding; Protein Structure, Tertiary; Serine Endopeptidases/chemistry; Serine Endopeptidases/metabolism; Serine Endopeptidases/ultrastructure; Viral Proteins/metabolism; Viral Proteins/ultrastructure |
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