Introduction
Eps1p, a S. cerevisiae disulfide chaperone, has a part in the ER-associated degradation machinary (PDB entry 4TVE). It is a unique member of the Protein Disulfide Isomerase family of proteins.
Exploring the Structure
Eps1 is a Trx-fold protein, with four Trx domains. It is a 75kDa protein made up of 701 amino acids. The , responsible for the fluorescent properties of the protein, is buried inside the beta barrel as part of the central alpha helix passing through the barrel. The chromophore forms via spontaneous cyclization and oxidation of three residues in the central alpha helix: -Thr65 (or Ser65)-Tyr66-Gly67. This cyclization and oxidation creates the chromophore's five-membered ring via a new bond between the threonine and the glycine residues[1].
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
