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Product disulfide oxidoreductase, periplasmic
| disulfide oxidoreductase, periplasmic |
| protein disulfide-isomerase |
PDI or PDI-like proteins act in the periplasm, and are located in periplasm or the inner membrane with active site facing periplasm. Oxidize diS bonds or rearrange wrongly paired diS bonds in exported proteins. By contrast,cytopl.more reducing.few diS's.
- Wunderlich, M., R. Jaenicke, R. Glockshuber 1993. The redox properties of protein disulfide isomerase (DsbA) of Escherichia coli result from a tense conformation of its oxidized form. J.Mol.Biol. 233:559-566
- Martin, J.L., J.C. Bardwell, J. Kuriyan 1993. Crystal structure of the DsbA protein required for disulphide bond formation in vivo. Nature 365:464-468
- Martin, J.L., G. Waksman, J.C. Bardwell, J.R. Beckwith, J. Kuriyan 1993. Crystallization of DsbA, an Escherichia coli protein required for disulphide bond formation in vivo. J.Mol.Biol. 230:1097-1100
- Zapun, A., J.C. Bardwell, T.E. Creighton 1993. The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo. Eur.J.Biochem. 32:5083-5092
- Wunderlich, M., A. Otto, R. Seckler, R. Glockshuber 1993. Bacterial protein disulfide isomerase: efficient catalysis of oxidative protein folding at acidic pH. Biochemistry 32:12251-12256
- Noiva, R 1994. Enzymatic catalysis of disulfide formation. Protein Expr. Purif. 5(1):1-13.
- Zapun, A., L. Cooper, T.E. Creighton 1994. Replacement of the active-site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo. Biochemistry 33:1907-1914
- Jacob-Dubuisson, F., J. Pinkner, Z. Xu, R. Striker, A. Padmanhaban, S.J. Hultgren 1994. PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbA. Proc.Natl.Acad.Sci.USA 91:11552-11556
- Joly, J.C., J.R. Swartz 1994. Protein folding activities of Escherichia coli protein disulfide isomerase. Biochemistry 33:4231-4236
- Nelson, J.W., T.E. Creighton 1994. Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo. Biochemistry 33:5974-5983
- McCarthy, A.A., P.W. Haebel, A. Torronen, V. Rybin, E.N. Baker, P. Metcalf 2000. Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli. Nat Struct Biol 7:196-199