3BOA
Crystal structure of yeast protein disulfide isomerase.
Summary for 3BOA
| Entry DOI | 10.2210/pdb3boa/pdb |
| Related | 1DSB 1EEJ 1MEK 2B5E 2BJX 2H8I |
| Descriptor | Protein disulfide-isomerase (1 entity in total) |
| Functional Keywords | disulfide bond formation, endoplasmic reticulum, molecular flexibility, protein folding, thioredoxin, glycoprotein, isomerase, redox-active center |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Cellular location | Endoplasmic reticulum lumen (Potential): P17967 |
| Total number of polymer chains | 1 |
| Total formula weight | 56421.61 |
| Authors | Tian, G.,Lennarz, W.J.,Schindelin, H. (deposition date: 2007-12-17, release date: 2008-09-23, Last modification date: 2024-10-30) |
| Primary citation | Tian, G.,Kober, F.X.,Lewandrowski, U.,Sickmann, A.,Lennarz, W.J.,Schindelin, H. The Catalytic Activity of Protein-disulfide Isomerase Requires a Conformationally Flexible Molecule. J.Biol.Chem., 283:33630-33640, 2008 Cited by PubMed Abstract: Protein-disulfide isomerase (PDI) catalyzes the formation of the correct pattern of disulfide bonds in secretory proteins. A low resolution crystal structure of yeast PDI described here reveals large scale conformational changes compared with the initially reported structure, indicating that PDI is a highly flexible molecule with its catalytic domains, a and a', representing two mobile arms connected to a more rigid core composed of the b and b' domains. Limited proteolysis revealed that the linker between the a domain and the core is more susceptible to degradation than that connecting the a' domain to the core. By restricting the two arms with inter-domain disulfide bonds, the molecular flexibility of PDI, especially that of its a domain, was demonstrated to be essential for the enzymatic activity in vitro and in vivo. The crystal structure also featured a PDI dimer, and a propensity to dimerize in solution and in the ER was confirmed by cross-linking experiments and the split green fluorescent protein system. Although sedimentation studies suggested that the self-association of PDI is weak, we hypothesize that PDI exists as an interconvertible mixture of monomers and dimers in the endoplasmic reticulum due to its high abundance in this compartment. PubMed: 18815132DOI: 10.1074/jbc.M806026200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.7 Å) |
Structure validation
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