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PMID:21736903
| Citation |
Baker, TA and Sauer, RT (2012) ClpXP, an ATP-powered unfolding and protein-degradation machine. Biochim. Biophys. Acta 1823:15-28 |
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| Abstract |
ClpXP is a AAA+ protease that uses the energy of ATP binding and hydrolysis to perform mechanical work during targeted protein degradation within cells. ClpXP consists of hexamers of a AAA+ ATPase (ClpX) and a tetradecameric peptidase (ClpP). Asymmetric ClpX hexamers bind unstructured peptide tags in protein substrates, unfold stable tertiary structure in the substrate, and then translocate the unfolded polypeptide chain into an internal proteolytic compartment in ClpP. Here, we review our present understanding of ClpXP structure and function, as revealed by two decades of biochemical and biophysical studies. |
| Links |
PubMed PMC3209554 Online version:10.1016/j.bbamcr.2011.06.007 |
| Keywords |
Adenosine Triphosphate/chemistry; Amino Acid Motifs; Catalytic Domain; Endopeptidase Clp/chemistry; Escherichia coli Proteins/chemistry; Humans; Hydrolysis; Protein Binding; Protein Interaction Domains and Motifs; Protein Structure, Quaternary; Protein Unfolding; Proteolysis |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0006508: proteolysis |
IEP: Inferred from Expression Pattern: |
P |
Figure 2 shows that under grow conditions where clpX is added, it inhibits the ftsZ protein which is the chief modulator of cell division. ftsZ degradation by clpX shows its proteolysis properties. |
complete |
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See also
References
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