dsbA Antibody

1. analysis of mutants that map to two areas in the structure of DsbB, one located between the two first transmembrane segments where the quinone ring binds and the other located in the second periplasmic loop of DsbB, which interacts with DsbA PMID: 28232484
2. DsbA and DsbL introduce the disulfide bond into unfolded bacterial aryl sulfotransferase (ASST) at similar rates. PMID: 24601529
3. A high-resolution structural model of integral membrane protein DsbB in E. coli is responsible for oxidizing the periplasmic protein DsbA, which forms disulfide bonds in substrate proteins. PMID: 23416557
4. Studies indicate that DsbA could effectively assist proteins folding, both in vivo coexpressed with the target protein, and in vitro replenished as foldases. PMID: 17366881
5. Conversion of the conserved cis proline 151 of DsbA to several hydrophilic residues results in accumulation of mixed disulfides between DsbA and its dedicated oxidant, DsbB. PMID: 15687218
6. Results describe the crystal structure of the DsbA mutant C33A at 2.0 angstroms resolution. PMID: 15755450
7. These results suggest that DsbA uses not only the signal recognition particle targeting pathway but also a special route of translocation through the translocon. PMID: 15937162
8. Results describbe the catalytic mechanism of DsbL, and provide evidence for proton shuffling during catalysis. PMID: 18692066
9. Study identified cotranslational and posttranslational folding intermediates of a periplasmic protein in which the protein and DsbA, a periplasmic disulfide bond-forming enzyme, are covalently linked by a disulfide bond. PMID: 19766568

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KEGG: ecj:JW3832

STRING: 316385.ECDH10B_4049