Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy-terminal tail

Likun Wang, Lei Wang, Stefano Vavassori, Shengjian Li, Huimin Ke, Tiziana Anelli, Massimo Degano, Riccardo Ronzoni, Roberto Sitia, Fei Sun, Chih Chen Wang

Research output: Contribution to journalArticle

Abstract

ERp44 mediates thiol-dependent retention in the early secretory pathway, forming mixed disulphides with substrate proteins through its conserved CRFS motif. Here, we present its crystal structure at a resolution of 2.6 Å. Three thioredoxin domains-a, b and b′-are arranged in a clover-like structure. A flexible carboxy-terminal tail turns back to the b′ and a domains, shielding a hydrophobic pocket in domain b′ and a hydrophobic patch around the CRFS motif in domain a. Mutational and functional studies indicate that the C-terminal tail gates the CRFS area and the adjacent hydrophobic pocket, dynamically regulating protein quality control.

Original languageEnglish
Pages (from-to)642-647
Number of pages6
JournalEMBO Reports
Volume9
Issue number7
DOIs
Publication statusPublished - Jul 2008

ASJC Scopus subject areas

  • Genetics
  • Cell Biology

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    Wang, L., Wang, L., Vavassori, S., Li, S., Ke, H., Anelli, T., Degano, M., Ronzoni, R., Sitia, R., Sun, F., & Wang, C. C. (2008). Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy-terminal tail. EMBO Reports, 9(7), 642-647. https://doi.org/10.1038/embor.2008.88