clpX Antibody

1. When the weak C-tag signal is replaced with a The AAA + unfoldase ClpX specifically recognizes two classes of recognition tags in the MuA transposase,specific features of these MuA tag classes direct ClpX to the biologically important reaction path. PMID: 25797169
2. the binding site of the ClpX dimeric cofactor, SspB2, on the zinc-binding domain (ZBD) in ClpX was determined by NMR and mutational analysis PMID: 17090685
3. These results support a major role for the RKH loops in substrate recognition and suggest that ClpX specificity represents an evolutionary compromise that has optimized degradation of multiple types of substrates rather than any single class. PMID: 17218279
4. The results support a model in which ClpX unfolding of GFP progresses via a metastable intermediate, which must be captured by several fast ATP-dependent translocation steps to prevent the protein from refolding and therefore escaping degradation. PMID: 18223658
5. Results reveal that the ssrA tag interacts with different loops that form the top, middle, and lower portions of the central channel of the ClpX hexamer. PMID: 18313382
6. Results describe how substrate multimerization modulates recognition by the ClpX unfoldase using a natural substrate, MuA transposase. PMID: 18406325
7. Results show that a tyrosine residue in a pore loop of the hexameric ClpX unfoldase links ATP hydrolysis to mechanical work by gripping substrates during unfolding and translocation. PMID: 18931677
8. The crystal structures presented here reveal striking asymmetry in ring hexamers of nucleotide-free and nucleotide-bound ClpX. PMID: 19914167

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KEGG: ecj:JW0428

STRING: 316385.ECDH10B_0394