clpA Antibody

1. These results suggest that the presence of gamma phosphate may serve to switch ClpA into a conformational state with high peptide binding activity, whereas affinity is severely attenuated when ADP is bound. PMID: 21376057
2. Molecular mechanism of polypeptide translocation catalyzed by the Escherichia coli ClpA protein translocase PMID: 20380838
3. one ClpS monomer is sufficient to direct the activity of the ClpA hexamer PMID: 20068042
4. identified a number of structural features in the N-domain, including a Zn(++) binding motif, several interfaces for binding to ClpS, and a prominent hydrophobic surface area that binds peptides in different configurations PMID: 15037248
5. determined structure at 12A resolution by cryo-electron microscopy; N-domain region is accentuated in a variance map of ClpAP and in a difference imaging experiment with ClpAP complexed with ClpS PMID: 15037249
6. ClpA has a single high affinity peptide binding site per hexamer PMID: 15657062
7. ClpA utilizes two structural elements, one in the N-temrinal domain and the other in the pore of the hexamer, both of which are required for efficient unfolding of some protein substrates. PMID: 18279386
8. Results suggest that the flexible attachment of the N-domains to ClpA allows their recruitment to the pore on demand for certain substrates, while allowing them to move out of the way for substrates binding directly to the pore. PMID: 18358489
9. Data support substrate translocation by ClpA via ATP-induced movements of the D2 loop. PMID: 18682217
10. Application of analytical ultracentrifugation and light scattering techniques reveals that ClpA self-associates in a monomer-tetramer equilibrium in the presence and absence of magnesium at 25 degrees centigrade. PMID: 19650643
11. ATP hydrolysis in both domains of ClpA was required for efficiently processing substrates of high local stability. PMID: 19726681

Show More

Hide All

KEGG: ecj:JW0866

STRING: 316385.ECDH10B_0952