5HQP

Crystal structure of the ERp44-peroxiredoxin 4 complex

Summary for 5HQP

• Entry DOI: 10.2210/pdb5hqp/pdb
• Related: 2R2J 3TJG 3TKP
• Descriptor: Peroxiredoxin-4, Endoplasmic reticulum resident protein 44 (3 entities in total)
• Functional Keywords: chaperone, gst fold, oxidoreductase, beta/alpha/beta sandwich, oxidoreductase-chaperone complex, oxidoreductase/chaperone
• Biological source: Homo sapiens (Human); More
• Cellular location: Cytoplasm : Q13162; Endoplasmic reticulum lumen: Q9BS26
• Total number of polymer chains: 4
• Total formula weight: 144386.11

Authors

Yang, K.,Li, D.F.,Wang, X.,Wang, C.C. (deposition date: 2016-01-22, release date: 2016-10-12, Last modification date: 2024-10-23)

Primary citation

Yang, K.,Li, D.F.,Wang, X.,Liang, J.,Sitia, R.,Wang, C.C.,Wang, X.
Crystal Structure of the ERp44-Peroxiredoxin 4 Complex Reveals the Molecular Mechanisms of Thiol-Mediated Protein Retention.
Structure, 24:1755-1765, 2016

PubMed Abstract: ERp44 controls the localization and transport of diverse proteins in the early secretory pathway. The mechanisms that allow client recognition and the source of the oxidative power for forming intermolecular disulfides are as yet unknown. Here we present the structure of ERp44 bound to a client, peroxiredoxin 4. Our data reveal that ERp44 binds the oxidized form of peroxiredoxin 4 via thiol-disulfide interchange reactions. The structure explains the redox-dependent recognition and characterizes the essential non-covalent interactions at the interface. The ERp44-Prx4 covalent complexes can be reduced by glutathione and protein disulfide isomerase family members in the ER, allowing the two components to recycle. This work provides insights into the mechanisms of thiol-mediated protein retention and indicates the key roles of ERp44 in this biochemical cycle to optimize oxidative folding and redox homeostasis.

PubMed: 27642162
DOI: 10.1016/j.str.2016.08.002

Experimental method

X-RAY DIFFRACTION (2.6 Å)