3WGX: Crystal Structure Of Erp46 Trx2 In A Complex With Prx4 C-term

The mammalian endoplasmic reticulum (ER) contains a diverse oxidative protein folding network in which ERp46, a member of the protein disulfide isomerase (PDI) family, serves as an efficient disulfide bond introducer together with Peroxiredoxin-4 (Prx4). We revealed a radically different molecular architecture of ERp46, in which the N-terminal two thioredoxin (Trx) domains with positively charged patches near their peptide-binding site and the C-terminal Trx are linked by unusually long loops and arranged extendedly, forming an opened V-shape. Whereas PDI catalyzes native disulfide bond formation by the cooperative action of two mutually facing redox-active sites on folding intermediates bound to the central cleft, ERp46 Trx domains are separated, act independently, and engage in rapid but promiscuous disulfide bond formation during early oxidative protein folding. Thus, multiple PDI family members likely contribute to different stages of oxidative folding and work cooperatively to ensure the efficient production of multi-disulfide proteins in the ER.
PDB ID: 3WGXDownload
MMDB ID: 120923
PDB Deposition Date: 2013/8/13
Updated in MMDB: 2014/06
Experimental Method:
x-ray diffraction
Resolution: 0.92  Å
Source Organism:
Mus musculus
Similar Structures:
Biological Unit for 3WGX: dimeric; determined by author and by software (PISA)
Molecular Components in 3WGX
Label Count Molecule
Proteins (2 molecules)
Thioredoxin Domain-containing Protein 5(Gene symbol: TXNDC5)
Molecule annotation
Peroxiredoxin-4(Gene symbol: Prdx4)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB