An unexpected co-crystal structure of the calpain PEF(S) domain with Hfq reveals a potential chaperone function of Hfq

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Abstract

Calpain is a Ca2+-activated, heterodimeric cysteine protease consisting of a large catalytic subunit and a small regulatory subunit. Dysregulation of this enzyme is involved in a range of pathological conditions such as cancer, Alzheimer's disease and rheumatoid arthritis, and thus calpain I is a drug target with potential therapeutic applications. Difficulty in the production of this enzyme has hindered structural and functional investigations in the past, although heterodimeric calpain I can be generated by Escherichia coli expression in low yield. Here, an unexpected structure discovered during crystallization trials of heterodimeric calpain I (CAPN1C115S + CAPNS1ΔGR) is reported. A novel co-crystal structure of the PEF(S) domain from the dissociated regulatory small subunit of calpain I and the RNA-binding chaperone Hfq, which was likely to be overproduced as a stress response to the recombinant expression conditions, was obtained, providing unexpected insight in the chaperone function of Hfq.
Original languageEnglish
Pages (from-to)81-85
Number of pages5
JournalActa Crystallographica. Section F: Structural Biology and Crystallization Communications
Volume76
Issue numberPt 2
DOIs
Publication statusPublished - 1 Feb 2020

Keywords

  • Calpain/chemistry
  • Crystallography, X-Ray
  • Host Factor 1 Protein/chemistry
  • Humans
  • Models, Molecular
  • Molecular Chaperones/chemistry
  • Protein Binding
  • Protein Conformation
  • Protein Domains
  • Protein Multimerization

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