4F9Z

Crystal Structure of human ERp27

Summary for 4F9Z

• Entry DOI: 10.2210/pdb4f9z/pdb
• Related: 2L4C
• Descriptor: Endoplasmic reticulum resident protein 27, ACETATE ION, 3,6,9,12,15,18,21,24,27,30,33,36,39-TRIDECAOXAHENTETRACONTANE-1,41-DIOL, ... (5 entities in total)
• Functional Keywords: thioredoxin fold, er foldase, erp57, endoplasmic reticulum, peptide binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Endoplasmic reticulum lumen: Q96DN0
• Total number of polymer chains: 5
• Total formula weight: 128430.64

Authors

Kober, F.X.,Koelmel, W.,Kuper, J.,Schindelin, H. (deposition date: 2012-05-21, release date: 2012-12-05, Last modification date: 2024-02-28)

Primary citation

Kober, F.X.,Koelmel, W.,Kuper, J.,Drechsler, J.,Mais, C.,Hermanns, H.M.,Schindelin, H.
The Crystal Structure of the Protein-Disulfide Isomerase Family Member ERp27 Provides Insights into Its Substrate Binding Capabilities.
J.Biol.Chem., 288:2029-2039, 2013

PubMed Abstract: About one-third of all cellular proteins pass through the secretory pathway and hence undergo oxidative folding in the endoplasmic reticulum (ER). Protein-disulfide isomerase (PDI) and related members of the PDI family assist in the folding of substrates by catalyzing the oxidation of two cysteines and isomerization of disulfide bonds as well as by acting as chaperones. In this study, we present the crystal structure of ERp27, a redox-inactive member of the PDI family. The structure reveals its substrate-binding cleft, which is homologous to PDI, but is able to adapt in size and hydrophobicity. Isothermal titration calorimetry experiments demonstrate that ERp27 is able to distinguish between folded and unfolded substrates, only interacting with the latter. ERp27 is up-regulated during ER stress, thus presumably allowing it to bind accumulating misfolded substrates and present them to ERp57 for catalysis.

PubMed: 23192347
DOI: 10.1074/jbc.M112.410522

Experimental method

X-RAY DIFFRACTION (2.2 Å)